protein Name cysteinedioxygenase, type I caption image width HGNCid 1795 Symbol CDO1 AltSymbols EntrezGene 1036 OMIM 603943 RefSeq NM 001801 UniProt Q16878 PDB ECnumber 1.13.11.20 Chromosome 5 Arm q Band 23.2 LocusSupplementaryData Cysteinedioxygenase CDO, CAS number 37256 59 0 is a mammalian non heme iron enzyme that catalyze s the conversion of L cysteine to cysteine sulfinic acid cysteine sulfinate by incorporation of dioxygen . Image Cysteinedioxygenase reaction.png frame none CDO reaction scheme showing cysteine sulfinic acid formation from cysteine by dioxygen incorporation Cysteine sulfinic acid lies at a branch point in cysteine catabolism , where it can follow two pathways resulting in the formation of taurine or sulfate . The cysteine sulfinic acid dependent pathway of taurine metabolism follows the synthesis of hypotaurine 2 aminoethane sulfinate , which is subsequently oxidized to taurine. Also, cysteine sulfinate can undergo transamination to form sulfinylpyruvate , decomposing to form pyruvate and sulfite . References cite journal author Sakakibara S, Yamaguchi K, Hosokawa Y, Kohashi N, Ueda I title Purification and some properties of rat liver cysteine oxidase cysteinedioxygenase journal Biochim. Biophys. Acta volume 422 issue 2 pages 273 9 year 1976 month February pmid 2307 doi url cite journal author Chai SC, Jerkins AA, Banik JJ, et al title Heterologous expression, purification, and characterization of recombinant rat cysteinedioxygenase journal J. Biol. Chem. volume 280 issue 11 pages 9865 9 year 2005 month March pmid 15623508 doi 10.1074 jbc.M413733200 url http www.jbc.org cgi pmidlookup?view long&pmid 15623508 cite journal author McCoy JG, Bailey LJ, Bitto E, et al title Structure and mechanism of mouse cysteinedioxygenase journal Proc. Natl. Acad. Sci. U.S.A. volume 103 issue 9 pages 3084 9 year 2006 month February pmid 16492780 pmc 1413891 doi 10.1073 pnas.0509262103 url http www.pnas.org cgi pmidlookup?view long&pmid 16492780 1.13 enzyme ... more details
Infobox protein family Symbol Dioxygenase C Name Dioxygenase image PDB 1eob EBI.jpg width caption crystal structure of acinetobacter sp. adp1 protocatechuate 3,4 dioxygenase in complex with 3,4 dihydroxybenzoate Pfam PF00775 Pfam clan CL0287 InterPro IPR000627 SMART PROSITE PDOC00079 MEROPS SCOP 2pcd TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol Dioxygenase N Name Catechol dioxygenase N terminus image PDB 1s9a EBI.jpg width caption crystal structure of 4 chlorocatechol 1,2 dioxygenase from rhodococcus opacus 1cp Pfam PF04444 Pfam clan InterPro IPR007535 SMART PROSITE MEROPS SCOP 1dlm TCDB OPM family OPM protein CAZy CDD In molecular biology, a dioxygenase is an enzyme which catalyse s the incorporation of both atom s of oxygen molecular oxygen into substrate biochemistry substrates using a variety of reaction mechanism s. Bond cleavage Cleavage of aromatic rings is one of the most important functions of dioxygenases, which play key roles in the Chemical decomposition degradation of aromatic compounds . The Enzyme substrate substrate s of ring cleavage dioxygenases can be classified into two groups according to the mode of scission of the aromatic ring. Intradiol enzyme s use a non haem Fe III to bond cleavage cleave the aromatic ring between two hydroxyl groups ortho cleavage , whereas extradiol enzymes use a non haem Fe II to cleave the aromatic ring between a hydroxylated carbon and an adjacent non hydroxylated carbon meta cleavage . ref name pmid10730195 cite journal author Broderick JB title Catechol dioxygenases journal Essays Biochem. volume 34 issue ... dioxygenase 1,2 CTD EC number 1.3.11.1 protocatechuate 3,4 dioxygenase 3,4 PCD EC number 1.3.11.3 and chlorocatechol 1,2 dioxygenase EC number 1.3.11.1 ref name pmid15060064 cite journal author Ferraroni ... of 4 chlorocatechol 1,2 dioxygenase from the chlorophenol utilizing gram positive Rhodococcus opacus ... 2,3 dioxygenase 2,3 CTD EC number 1.3.11.2 and biphenyl 2,3 diol 1,2 dioxygenase BphC EC number ... more details
Unreferenced date December 2009 Cysteine metabolism refers to the biological pathways that consume or create cysteine . The pathways of different amino acids and other metabolites interweave and overlap to creating complex systems. Human cysteine metabolism In human cysteine metabolism, L cysteine is consumed in several ways as shown below. L cysteine is also consumed in methionine and glutathione metabolism as well as pantothenate CoA biosynthesis. class wikitable style text align center L cysteine consumption pathways enzyme product cysteinedioxygenase 3 sulfino L alanine or cysteine sulfinic acid amino acid racemase D cysteinecysteine lyase L cysteate cysteine tRNA ligase L cysteinyl tRNA sup Cys sup cystine reductase L cystine cysteine transaminase 3 mercapto pyruvate L cysteine is the product of several processes as well. In addition to the reactions below, L cysteine is also a product of glycine , serine , and threonine metabolism. class wikitable style text align center L cysteine production pathways starting chemical enzyme O acetyl L serine cysteine synthase L cystine glutathione cystine transhydrogenase pyruvate cystathionine lyase 3 mercapto pyruvate cysteine transaminase See also D cysteine desulfhydrase Sulphur metabolism DEFAULTSORT Cysteine Metabolism Category Sulfur metabolism Category Sulfur amino acids ja ... more details
DISPLAYTITLE S Allyl cysteine chembox verifiedrevid 401045767 Name S Allyl cysteine ImageFile Allyl cysteine.png ImageSize 200px ImageName S Allyl cysteine ImageFile1 S allyl cysteine 3D balls.png ImageSize1 200px ImageName1 S Allyl cysteine IUPACName R 2 Amino 3 prop 2 enylsulfanylpropanoic acid OtherNames S 2 propenyl small L small cysteine S allyl laevo cysteine S allylcysteine Section1 Chembox Identifiers Abbreviations SAC InChI 1 C6H13NO2S c1 2 3 10 4 5 7 6 8 9 h2,5 6,8 9H,1,3 4,7H2 t5 m0 s1 InChIKey WRHLYKLSIBWCTJ YFKPBYRVBK StdInChI Ref stdinchicite correct chemspider StdInChI 1S C6H13NO2S c1 2 3 10 4 5 7 6 8 9 h2,5 6,8 9H,1,3 4,7H2 t5 m0 s1 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey WRHLYKLSIBWCTJ YFKPBYRVSA N CASNo 21593 77 1 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 21106477 SMILES OC O C H N CSCC C Section2 Chembox Properties Formula C sub 6 sub H sub 11 sub NO sub 2 sub S MolarMass 161.22 g mol Density 1.191 0.06 g cm sup 3 sup MeltingPt 219 220 C S Allyl cysteine SAC is an organic compound that is a natural constituent of fresh garlic . It is a derivative of the amino acid cysteine in which an allyl group has been added to the sulfur atom. Allyl cysteine is currently being investigated as a potential cholesterol lowering agent ref cite journal author Yeh Y Y Liu L title Cholesterol lowering effect of garlic extracts and organosulfur compounds human and animal studies journal Journal of Nutrition year 2001 volume 131 issue 3s pages 989S 93S pmid 11238803 ref and as a chemopreventive. ref cite journal doi 10.2174 1573394054021772 author Arora, Annu Tripathi, Chitra Shukla, Yogeshwer title Garlic and its organosulfides as potential ... 2 pages 199 205 ref See also Alliin , the S oxide of allyl cysteine References reflist External links http www.thegoodscentscompany.com data rw1593931.html S allyl laevo cysteine , thegoodscentscompany.com DEFAULTSORT Allyl cysteine, S Category Sulfur amino acids Category Antioxidants Category Thioethers ... more details
enzyme Name cysteine desulfurase EC number 2.8.1.7 CAS number IUBMB EC number 2 8 1 7 GO code 0031071 image width caption In enzymology , a cysteine desulfurase EC number 2.8.1.7 is an enzyme that catalysis catalyzes the chemical reaction L cysteine enzyme cysteine math rightleftharpoons math L alanine enzyme S sulfanylcysteine Thus, the two substrate biochemistry substrates of this enzyme are L cysteine and enzyme cysteine , whereas its two product chemistry products are L alanine and enzyme S sulfanylcysteine . This enzyme belongs to the family of transferase s, specifically the sulfurtransferases, which transfer sulfur containing groups. The systematic name of this enzyme class is L cysteine enzyme cysteine sulfurtransferase . Other names in common use include IscS , NIFS , NifS , SufS , and cysteine desulfurylase . This enzyme participates in thiamine metabolism . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1T3I . References reflist 1 cite journal author Zheng L, White RH, Cash VL, Jack RF, Dean DR date 1993 title Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis journal Proc. Natl. Acad. Sci. U. S. A. volume 90 pages 2754&ndash 8 pmid 8464885 doi 10.1073 pnas.90.7.2754 issue 7 pmc 46174 cite journal author Mihara H, Esaki N date 2002 title Bacterial cysteine desulfurases their function and mechanisms journal Appl. Microbiol. Biotechnol. volume 60 pages 12&ndash 23 pmid 12382038 doi 10.1007 s00253 002 1107 4 issue 1 2 cite journal author Frazzon J, Dean DR date 2003 title Formation of iron sulfur clusters in bacteria an emerging field in bioinorganic chemistry journal Curr. Opin. Chem. Biol. volume 7 pages 166&ndash 73 pmid 12714048 doi 10.1016 S1367 5931 03 00021 8 issue 2 transferase stub Category EC 2.8.1 Category Enzymes of known structure ... more details
enzyme Name cysteine lyase EC number 4.4.1.10 CAS number 9079 86 1 IUBMB EC number 4 4 1 10 GO code 0047803 image width caption In enzymology , a cysteine lyase EC number 4.4.1.10 is an enzyme that catalysis catalyzes the chemical reaction L cysteine sulfite math rightleftharpoons math L cysteate hydrogen sulfide Thus, the two substrate biochemistry substrates of this enzyme are L cysteine and sulfite , whereas its two product chemistry products are L cysteate and hydrogen sulfide . This enzyme belongs to the family of lyase s, specifically the class of carbon sulfur lyases. The systematic name of this enzyme class is L cysteine hydrogen sulfide lyase adding sulfite L cysteate forming . Other names in common use include cysteine sulfite lyase , and L cysteine hydrogen sulfide lyase adding sulfite . This enzyme participates in cysteine metabolism and taurine and hypotaurine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Tolosa EA, Chepurnova NK, Khomutov RM, Severin ES date 1969 title Reactions catalysed by cysteine lyase from the yolk sac of chicken embryo journal Biochim. Biophys. Acta. volume 171 pages 369&ndash 71 pmid 5813025 issue 2 lyase stub Category EC 4.4.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ja ... more details
enzyme Name cysteine transaminase EC number 2.6.1.3 CAS number 9030 32 4 IUBMB EC number 2 6 1 3 GO code 0047801 image width caption In enzymology , a cysteine transaminase EC number 2.6.1.3 is an enzyme that catalysis catalyzes the chemical reaction L cysteine 2 oxoglutarate math rightleftharpoons math mercaptopyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L cysteine and 2 oxoglutarate , whereas its two product chemistry products are mercaptopyruvate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L cysteine 2 oxoglutarate aminotransferase . Other names in common use include cysteine aminotransferase , L cysteine aminotransferase , and CGT . This enzyme participates in cysteine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author CHATAGNER F, SAURET IGNAZI G date Paris title Role of transamination and pyridoxal phosphate in the enzymatic formation of hydrogen sulfide from cysteine by the rat liver under anaerobiosis. journal Bull. Soc. Chim. volume Biol. pages 415&ndash 28 pmid 13342749 issue 2 3 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ja ... more details
refimprove date January 2011 Infobox protein family Symbol Peptidase C1 Name Cysteine Peptidase image Papain enzyme.png width caption Crystal structure of the cysteine peptidase papain in complex with its ... s are enzyme s that degrade protein polypeptides . Cysteine proteases have a common catalysis catalytic mechanism that involves a nucleophile nucleophilic cysteine thiol in a catalytic dyad. The first ... protonated cysteine s anion ic sulfur on the Substrate biochemistry substrate carbonyl carbon ... carboxy terminus of the substrate to the cysteine thiol is formed. Therefore they are also sometimes ... . Cysteine proteases are commonly encountered in fruits including papaya , pineapple , Common fig ..., dozens of latex latices of different plant Family biology families are known to contain cysteine proteases ... ref Cysteine proteases are used as an ingredient in meat tenderizer s. Image Cysteinprotease Reaktionsmechanismus.svg thumb 300px Reaction mechanism of the cysteine protease mediated cleavage of a peptide bond. TOC Biological importance Cysteine proteases play multi faceted roles, virtually in every ... role of plant cysteine proteinases journal Acta Biochim Polonica. volume 51 issue 38 pages ... C, Gomes TMR, Hernandez M, Lopes MTP title Plant cysteine proteinases Evaluation of the pharmacological ... development. The ability of macrophages and other cells to mobilize elastolytic cysteine proteases ... journal author Chapman HA, Riese RJ, Shi GP. title Emerging roles of cysteine proteases in human biology ... . Plant cysteine proteinases isolated from these plants have been found to have high proteolysis .... ref cite journal author Stepek G, Behnke JM, Buttle DJ, Duce IR. title Natural plant cysteine proteinases ..., Buttle DJ, Stepek G, Lowe A, Duce IR. title Developing novel anthelmintics from plant cysteine proteinases ... www.biomedcentral.com content pdf 1756 3305 1 29.pdf ref Examples of cysteine proteases Actinidain ... cgi bin family index?type P C Cysteine Peptidases MeshName Cysteine endopeptidases ... more details
enzyme Name cysteine synthase EC number 2.5.1.47 CAS number 37290 89 4 IUBMB EC number 2 5 1 47 GO code 0004124 image width caption In enzymology , a cysteine synthase EC number 2.5.1.47 is an enzyme that catalysis catalyzes the chemical reaction O sub 3 sub acetyl L serine hydrogen sulfide math rightleftharpoons math L cysteine acetate Thus, the two substrate biochemistry substrates of this enzyme are O3 acetyl L serine and hydrogen sulfide , whereas its two product chemistry products are L cysteine and acetate . This enzyme belongs to the family of transferase s, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O3 acetyl L serine hydrogen sulfide 2 amino 2 carboxyethyltransferase . Other names in common use include O acetyl L serine sulfhydrylase , O acetyl L serine sulfohydrolase , O acetylserine thiol lyase , O acetylserine thiol lyase A , O acetylserine sulfhydrylase , O3 acetyl L serine acetate lyase adding hydrogen sulfide , acetylserine sulfhydrylase , cysteine synthetase , S sulfocysteine synthase , 3 O acetyl L serine hydrogen sulfide , and 2 amino 2 carboxyethyltransferase . This enzyme participates in 3 metabolism metabolic pathways cysteine metabolism , selenoamino acid metabolism , and sulfur metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 12 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1O58 , PDB link 1VE1 , PDB link 1Y7L , PDB link 1Z7W , PDB link 1Z7Y , PDB link 2BHS , PDB link 2BHT , PDB link 2EGU , PDB link 2ISQ , PDB link 2Q3B , PDB link 2Q3C , and PDB link 2Q3D . References reflist 1 cite journal author Becker MA, Kredich NM, Tomkins ... and Murakoshi I date 1987 title Difference between uracilylalanine synthases and cysteine synthases ... F date 1986 title Enzymatic synthesis of the neuroexcitatory amino acid quisqualic by cysteine synthase ... more details
enzyme Name taurine dioxygenase EC number 1.14.11.17 CAS number IUBMB EC number 1 14 11 17 GO code 0000908 image width caption In enzymology , a taurine dioxygenase EC number 1.14.11.17 is an enzyme that catalysis catalyzes the chemical reaction taurine 2 oxoglutarate O sub 2 sub math rightleftharpoons math sulfite aminoacetaldehyde succinate CO sub 2 sub The 3 substrate biochemistry substrates of this enzyme are taurine , 2 oxoglutarate , and oxygen O sub 2 sub , whereas its 4 product chemistry products are sulfite , aminoacetaldehyde , succinate , and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2 oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is taurine, 2 oxoglutarate O2 oxidoreductase sulfite forming . Other names in common use include 2 aminoethanesulfonate dioxygenase , and alpha ketoglutarate dependent taurine dioxygenase . This enzyme participates in taurine and hypotaurine metabolism . It has 3 cofactor biochemistry cofactors iron , Ascorbate , and Fe2 . Structural studies As of late 2007, 4 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1GQW , PDB link 1GY9 , PDB link 1OS7 , and PDB link 1OTJ . References reflist 1 cite journal author Eichhorn E, van der Ploeg JR, Kertesz MA, Leisinger T date 1997 title Characterization of alpha ketoglutarate dependent taurine dioxygenase from Escherichia coli journal J. Biol. Chem. volume 272 pages 23031&ndash 6 pmid 9287300 doi 10.1074 jbc.272.37.23031 issue 37 1.14 enzyme stub Category EC 1.14.11 Category Iron enzymes Category Ascorbate enzymes Category Fe2 enzymes Category Enzymes of known structure it Taurina diossigenasi ja ... more details
enzyme Name trimethyllysine dioxygenase EC number 1.14.11.8 CAS number 74622 49 4 IUBMB EC number 1 14 11 8 GO code 0050353 image width caption In enzymology , a trimethyllysine dioxygenase EC number 1.14.11.8 is an enzyme that catalysis catalyzes the chemical reaction N sub 6 sub ,N sub 6 sub ,N sub 6 sub trimethyl L lysine 2 oxoglutarate O sub 2 sub math rightleftharpoons math 3 hydroxy N sub 6 sub ,N sub 6 sub ,N sub 6 sub trimethyl L lysine succinate CO sub 2 sub The 3 substrate biochemistry substrates of this enzyme are N6,N6,N6 trimethyl L lysine , 2 oxoglutarate , and oxygen O sub 2 sub , whereas its 3 product chemistry products are 3 hydroxy N6,N6,N6 trimethyl L lysine , succinate , and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2 oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is N6,N6,N6 trimethyl L lysine,2 oxoglutarate oxygen oxidoreductase 3 hydroxylating . Other names in common use include trimethyllysine alpha ketoglutarate dioxygenase , TML alpha ketoglutarate dioxygenase , TML hydroxylase , 6 N,6 N,6 N trimethyl L lysine,2 oxoglutarate oxygen oxidoreductase , and 3 hydroxylating . This enzyme participates in lysine degradation . It has 3 cofactor biochemistry cofactors iron , Ascorbate , and Fe2 . References reflist 1 cite journal author Hulse JD, Ellis SR, Henderson LM date 1978 title Carnitine biosynthesis. beta Hydroxylation of trimethyllysine by an alpha ketoglutarate dependent mitochondrial dioxygenase journal J. Biol. Chem. volume 253 pages 1654&ndash 9 pmid 627563 issue 5 1.14 enzyme stub Category Human 2OG oxygenases Category EC 1.14.11 Category Iron enzymes Category Ascorbate enzymes Category Enzymes of unknown structure it Trimetillisina diossigenasi ja ... more details
enzyme Name 3 phenylpropanoate dioxygenase EC number 1.14.12.19 CAS number IUBMB EC number 1 14 12 19 GO code image width caption orphan date December 2008 In enzymology , a 3 phenylpropanoate dioxygenase EC number 1.14.12.19 is an enzyme that catalysis catalyzes the chemical reaction 3 phenylpropanoate NADH H sup sup O sub 2 sub math rightleftharpoons math 3 cis 5,6 dihydroxycyclohexa 1,3 dien 1 yl propanoate NAD sup sup The 4 substrate biochemistry substrates of this enzyme are 3 phenylpropanoate , nicotinamide adenine dinucleotide NADH , hydrogen ion H sup sup , and oxygen O sub 2 sub , whereas its two product chemistry products are 3 cis 5,6 dihydroxycyclohexa 1,3 dien 1 yl propanoate and nicotinamide adenine dinucleotide NAD sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is 3 phenylpropanoate,NADH oxygen oxidoreductase 2,3 hydroxylating . Other names in common use include HcaA1A2CD , Hca dioxygenase , and 3 phenylpropionate dioxygenase . References reflist 1 cite journal author Diaz E, Ferrandez A, Garcia JL date 1998 title Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3 phenylpropionic acid in Escherichia coli K 12 journal J. Bacteriol. volume 180 pages 2915&ndash 23 pmid 9603882 issue 11 pmc 107259 cite journal author Burlingame R, Chapman PJ date 1983 title Catabolism of phenylpropionic acid and its 3 hydroxy derivative by Escherichia coli journal J. Bacteriol. volume 155 pages 113&ndash 21 pmid 6345502 issue 1 pmc 217659 Category EC 1.14.12 Category NADPH dependent enzymes Category NADH dependent enzymes Category Enzymes of unknown structure 1.14 enzyme stub it 3 fenilpropanoato diossigenasi ja 3 ... more details
enzyme Name toluene dioxygenase EC number 1.14.12.11 CAS number 120038 36 0 IUBMB EC number 1 14 12 11 GO code 0018624 image width caption In enzymology , a toluene dioxygenase EC number 1.14.12.11 is an enzyme that catalysis catalyzes the chemical reaction toluene NADH H sup sup O sub 2 sub math rightleftharpoons math 1S,2R 3 methylcyclohexa 3,5 diene 1,2 diol NAD sup sup The 4 substrate biochemistry substrates of this enzyme are toluene , nicotinamide adenine dinucleotide NADH , hydrogen ion H sup sup , and oxygen O sub 2 sub , whereas its two product chemistry products are 1S,2R 3 methylcyclohexa 3,5 diene 1,2 diol and nicotinamide adenine dinucleotide NAD sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is toluene,NADH oxygen oxidoreductase 1,2 hydroxylating . This enzyme is also called toluene 2,3 dioxygenase . This enzyme participates in toluene and xylene degradation . References reflist 1 cite journal author Renganathan V date 1989 title Possible involvement of toluene 2,3 dioxygenase in defluorination of 3 fluoro substituted benzenes by toluene degrading Pseudomonas sp strain T 12 journal Appl. Exp. Microbiol. volume 55 pages 330&ndash 334 cite journal author Subramanian V, Liu TN, Yeh WK, Gibson DT date 1979 title Toluene dioxygenase purification of an iron sulfur protein by affinity chromatography journal Biochem. Biophys. Res. Commun. volume 91 pages 1131&ndash 9 pmid 526270 doi 10.1016 0006 291X 79 91998 3 issue 3 1.14 enzyme stub Category EC 1.14.12 Category NADPH dependent enzymes Category NADH dependent enzymes Category Enzymes of unknown structure it Toluene diossigenasi ja ... more details
enzyme Name 3 hydroxy 2 methylpyridinecarboxylate dioxygenase EC number 1.14.12.4 CAS number 37256 69 2 IUBMB EC number 1 14 12 4 GO code 0047081 image width caption In enzymology , a 3 hydroxy 2 methylpyridinecarboxylate dioxygenase EC number 1.14.12.4 is an enzyme that catalysis catalyzes the chemical reaction 3 hydroxy 2 methylpyridine 5 carboxylate NAD P H H sup sup O sub 2 sub math rightleftharpoons math 2 acetamidomethylene succinate NAD P The 5 substrate biochemistry substrates of this enzyme are 3 hydroxy 2 methylpyridine 5 carboxylate , nicotinamide adenine dinucleotide NADH , nicotinamide adenine dinucleotide phosphate NADPH , hydrogen ion H sup sup , and oxygen O sub 2 sub , whereas its 3 product chemistry products are 2 acetamidomethylene succinate , nicotinamide adenine dinucleotide NAD sup sup , and nicotinamide adenine dinucleotide phosphate NADP sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor. The systematic name of this enzyme class is 3 hydroxy 2 methylpyridine 5 carboxylate,NAD P H oxygen oxidoreductase decyclizing . Other names in common use include methylhydroxypyridinecarboxylate oxidase , 2 methyl 3 hydroxypyridine 5 carboxylic acid dioxygenase , methylhydroxypyridine carboxylate dioxygenase , and 3 hydroxy 3 methylpyridinecarboxylate dioxygenase incorrect . This enzyme participates in vitamin B6 vitamin B sub 6 sub metabolism . It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author Sparrow LG, Ho PP, Sundaram TK, Zach D, Nyns EJ, Snell EE date 1969 title The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3 hydroxypyridine ring journal J. Biol. Chem. volume 244 pages ... more details
enzyme Name thymine dioxygenase EC number 1.14.11.6 CAS number 37256 67 0 IUBMB EC number 1 14 11 6 GO code 0050341 image width caption In enzymology , a thymine dioxygenase EC number 1.14.11.6 is an enzyme that catalysis catalyzes the chemical reaction thymine 2 oxoglutarate O sub 2 sub math rightleftharpoons math 5 hydroxymethyluracil succinate CO sub 2 sub The 3 substrate biochemistry substrates of this enzyme are thymine , 2 oxoglutarate , and oxygen O sub 2 sub , whereas its 3 product chemistry products are 5 hydroxymethyluracil , succinate , and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2 oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is thymine,2 oxoglutarate oxygen oxidoreductase 7 hydroxylating . Other names in common use include thymine 7 hydroxylase , 5 hydroxy methyluracil dioxygenase , and 5 hydroxymethyluracil oxygenase . It has 2 cofactor biochemistry cofactors iron , and Ascorbate . References reflist 1 cite journal author Bankel L, Holme E, Lindstedt G, Lindstedt S date 1972 title Oxygenases involved in thymine and thymidine metabolism in Neurospora crassa journal FEBS. Lett. volume 21 pages 135&ndash 138 pmid 11946494 doi 10.1016 0014 5793 72 80121 2 issue 2 cite journal author Liu CK, Hsu CA, Abbott MT date 1973 title Catalysis of three sequential dioxygenase reactions by thymine 7 hydroxylase journal Arch. Biochem. Biophys. volume 159 pages 180&ndash 7 pmid 4274083 doi 10.1016 0003 9861 73 90443 8 issue 1 cite journal author Warn Cramer BJ, Macrander LA, Abbott MT date 1983 title Markedly different ascorbate dependencies of the sequential alpha ketoglutarate dioxygenase reactions catalyzed by an essentially homogeneous thymine 7 hydroxylase from Rhodotorula glutinis journal ... more details
enzyme Name 2 nitropropane dioxygenase EC number 1.13.11.32 CAS number 65802 82 6 IUBMB EC number 1 13 11 32 GO code 0018580 image width caption In enzymology , a 2 nitropropane dioxygenase EC number 1.13.11.32 is an enzyme that catalysis catalyzes the chemical reaction 2 2 nitropropane O sub 2 sub math rightleftharpoons math 2 acetone 2 nitrite Thus, the two substrate biochemistry substrates of this enzyme are 2 nitropropane and oxygen O sub 2 sub , whereas its two product chemistry products are acetone and nitrite . This enzyme belongs to the family of oxidoreductase s, specifically those acting on single donors with O sub 2 sub as oxidant and incorporation of two atoms of oxygen into the substrate oxygenases . The oxygen incorporated need not be derived from O sub 2 sub . The systematic name of this enzyme class is 2 nitropropane oxygen 2 oxidoreductase . This enzyme participates in nitrogen metabolism . It has 3 cofactor biochemistry cofactors FAD , Iron , and FMN . Structural studies As of late 2007 Steve Fuhrer from the DHPA solved this very complex formula to find, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2GJL and PDB link 2GJN . References reflist 1 cite journal author Kido T, Soda K, Suzuki T, Asada K year 1976 title A new oxygenase, 2 nitropropane dioxygenase of Hansenula mrakii Enzymologic and spectrophotometric properties journal J. Biol. Chem. volume 251 pages 6994&ndash 7000 pmid 11214 issue 22 cite journal author Yoon HJ, Suh SW year 2006 title Crystal structure of 2 nitropropane dioxygenase complexed with FMN and substrate. Identification of the catalytic base journal J. Biol. Chem. volume 281 pages 18660&ndash 7 pmid 16682407 doi 10.1074 jbc.M601658200 issue 27 cite journal author Francis K, Russell B, Gadda G year 2005 title Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2 nitropropane dioxygenase journal J. Biol. Chem ... more details
Refimprove date June 2007 Protein Name 4 hydroxyphenylpyruvate dioxygenase Symbol HPPD AltSymbols HPD PPD HGNCid 5147 Chromosome 12 Arm q Band 24 qter LocusSupplementaryData ECnumber 1.13.11.27 OMIM 609695 EntrezGene 3242 RefSeq NM 002150 UniProt P32754 File 1SP9 Ribbon.png 237 px right thumb Homodimer of 4 Hydroxyphenylpyruvate dioxygenase. Red ribbon represents iron containing catalytic domain with Fe 2 represented as red orange spheres blue represents the oligomeric domain. Image generated from published structural data ref cite journal last Fritze first I.M. coauthors Freigang, J., Auerbach, G., Huber, R., Steinbacher, S. title The Crystal Structures of Zea mays and Arabidopsis 4 Hydroxyphenylpyruvate Dioxygenase journal Plant Physiol. year 2004 volume 134 pages 1388 1400 doi 10.1104 pp.103.034082 pmc 419816 issue 4 pmid 15084729 rendered with UCSF Chimera http plato.cgl.ucsf.edu chimera ref 4 Hydroxyphenylpyruvate dioxygenase HPPD is an iron Fe containing enzyme , that catalyzes the second chemical reaction reaction in the catabolism of tyrosine the conversion of 4 hydroxyphenylpyruvate to homogentisate . Function The HPPD reaction occurs through a NIH shift and involves the oxidative decarboxylation of an oxo acid as well as aromatic ring hydroxylation . The NIH shift, which has been demonstrated through isotope labeling studies, involves migration of an alkyl group to form a more stable carbocation . The shift, accounts for the observation that C3 is bonded to C4 in 4 hydroxyphenylpyruvate but to C5 in homogentisate. br style clear both See also 4 hydroxyphenylpyruvate hydroxylase deficiency Alpha keto acid dependent dioxygenases Amino acid metabolism enzymes ref cite journal last1 Saito first1 I last2 Chujo first2 Y last3 Shimazu first3 H last4 Yamane first4 M last5 Matsuura first5 T title Nonenzymic oxidation of p hydroxyphenylpyruvic acid with singlet oxygen ... pyruvate dioxygenase from Streptomyces avermitilis the basis for ordered substrate addition journal ... more details
enzyme Name cysteamine dioxygenase EC number 1.13.11.19 CAS number 9033 41 4 IUBMB EC number 1 13 11 19 GO code 0047800 image width caption In enzymology , a cysteamine dioxygenase EC number 1.13.11.19 is an enzyme that catalysis catalyzes the chemical reaction 2 aminoethanethiol O sub 2 sub math rightleftharpoons math hypotaurine Thus, the two substrate biochemistry substrates of this enzyme are 2 aminoethanethiol and oxygen O sub 2 sub , whereas its product chemistry product is hypotaurine . This enzyme belongs to the family of oxidoreductase s, specifically those acting on single donors with O sub 2 sub as oxidant and incorporation of two atoms of oxygen into the substrate oxygenases . The oxygen incorporated need not be derived from O sub 2 sub . The systematic name of this enzyme class is 2 aminoethanethiol oxygen oxidoreductase . Other names in common use include persulfurase , cysteamine oxygenase , and cysteamine oxygen oxidoreductase . This enzyme participates in taurine and hypotaurine metabolism . It employs one cofactor biochemistry cofactor , iron . References reflist 1 cite journal author Cavallini D, De Marco C, Scandurra R, Dupre S, Graziani MT date 1966 title The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme journal J. Biol. Chem. volume 241 pages 3189&ndash 96 pmid 5912113 issue 13 cite journal author Wood JL, Cavallini D date 1967 title Enzymic oxidation of cysteamine to hypotaurine in the absence of a cofactor journal Arch. Biochem. Biophys. volume 119 pages 368&ndash 72 pmid 6052430 doi 10.1016 0003 9861 67 90467 5 issue 1 cite journal author Cavallini D, Federici G, Ricci G, Dupre S, Antonucci A date 1975 title The specificity of cysteamine oxygenase journal FEBS Lett. volume 56 pages 348&ndash 51 pmid 1157952 doi 10.1016 0014 5793 75 81124 0 issue 2 cite journal author Richerson RB, Ziegler DM date 1987 ... doi 10.1016 0076 6879 87 43071 1 chapter Cysteamine dioxygenase series Methods in Enzymology isbn ... more details
enzyme Name 5 pyridoxate dioxygenase EC number 1.14.12.5 CAS number 37256 70 5 IUBMB EC number 1 14 12 5 GO code 0047592 image width caption In enzymology , a 5 pyridoxate dioxygenase EC number 1.14.12.5 is an enzyme that catalysis catalyzes the chemical reaction 3 hydroxy 4 hydroxymethyl 2 methylpyridine 5 carboxylate NADPH H sup sup O sub 2 sub math rightleftharpoons math 2 acetamidomethylene 3 hydroxymethyl succinate NADP sup sup The 4 substrate biochemistry substrates of this enzyme are 3 hydroxy 4 hydroxymethyl 2 methylpyridine 5 carboxylate , nicotinamide adenine dinucleotide phosphate NADPH , hydrogen ion H sup sup , and oxygen O sub 2 sub , whereas its two product chemistry products are 2 acetamidomethylene 3 hydroxymethyl succinate and nicotinamide adenine dinucleotide phosphate NADP sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is 5 pyridoxate,NADPH oxygen oxidoreductase decyclizing . This enzyme is also called 5 pyridoxate oxidase . This enzyme participates in vitamin B6 vitamin B sub 6 sub metabolism . It has 2 cofactor biochemistry cofactors FAD , and Flavoprotein . References reflist 1 cite journal author Sparrow LG, Ho PP, Sundaram TK, Zach D, Nyns EJ, Snell EE date 1969 title The bacterial oxidation of vitamin B6. VII. Purification, properties, and mechanism of action of an oxygenase which cleaves the 3 hydroxypyridine ring journal J. Biol. Chem. volume 244 pages 2590&ndash 600 pmid 4306031 issue 10 1.14 enzyme stub Category EC 1.14.12 Category NADPH dependent enzymes Category Flavin enzymes Category Flavoprotein enzymes Category Enzymes of unknown structure it 5 piridossato diossigenasi ja 5 ... more details
enzyme Name gibberellin 44 dioxygenase EC number 1.14.11.12 CAS number 112198 85 3 IUBMB EC number 1 14 11 12 GO code 0047927 image width caption In enzymology , a gibberellin 44 dioxygenase EC number 1.14.11.12 is an enzyme that catalysis catalyzes the chemical reaction gibberellin 44 2 oxoglutarate O sub 2 sub math rightleftharpoons math gibberellin 19 succinate CO sub 2 sub The 3 substrate biochemistry substrates of this enzyme are gibberellin 44 , 2 oxoglutarate , and oxygen O sub 2 sub , whereas its 3 product chemistry products are gibberellin 19 , succinate , and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2 oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is gibberellin 44 ,2 oxoglutarate oxygen oxidoreductase . Other names in common use include oxygenase, gibberellin A44 oxidase , and gibberellin 44 , 2 oxoglutarate oxygen oxidoreductase . This enzyme participates in diterpenoid biosynthesis . It employs one cofactor biochemistry cofactor , iron . References reflist 1 cite journal author Gilmour SJ, Bleecker AB and Zeevaart JAD year 1987 title Partial purification of gibberellin oxidases from spinach leaves journal Plant Physiol. volume 85 pages 87&ndash 90 doi 10.1104 pp.85.1.87 pmid 16665690 issue 1 pmc 1054208 Category EC 1.14.11 Category Iron enzymes Category Enzymes of unknown structure 1.14 enzyme stub it Gibberellina 44 diossigenasi ja 44 ... more details
Catechol dioxygenases are metalloprotein enzyme s that carry out the oxidative cleavage of catechol s. This class of enzymes incorporate dioxygen into the substrate biochemistry . Catechol dioxygenases belong to the class of oxidoreductase s and have several different substrate specificities, including catechol 1,2 dioxygenase EC number 1.13.11.1 , catechol 2,3 dioxygenase EC number 1.13.11.2 , and protocatechuate 3,4 dioxygenase EC number 1.13.11.3 . The active site of catechol dioxygenases most frequently contains iron , but manganese containing forms are also known. The Pseudomonas putida xylE gene, which encodes catechol 2,3 dioxygenase, is often used as a reporter to quantitate gene expression. An example of the reaction carried out by catechol 1,2 dioxygenase is the formation of muconic acid cis,cis muconic acid from catechol , shown below. Image Catachol dioxygenase reaction.png frame center See also Bioinorganic chemistry Oxygenase References Stephen J. Lippard, Jeremy M. Berg, Principles of Bioinorganic Chemistry , University Science Books, 1994, ISBN 0 935702 72 5 J.J.R. Fra sto da Silva and R.J.P. Williams, The biological chemistry of the elements The inorganic chemistry of life , 2nd Edition, Oxford University Press, 2001, ISBN 0 19 850848 4 Category Enzymes Category Oxidoreductases Category EC 1.13.11 1.13 enzyme stub Monooxygenases ja ... more details
chembox verifiedrevid 433880904 ImageFile 3 Sulfino L alanine.svg ImageSize ImageName Skeletal formula ImageFile1 L Cysteine sulfinic acid 3D balls.png ImageSize1 150px ImageName1 Ball and stick model IUPACName 2 amino 3 sulfinopropanoic acid OtherNames Section1 Chembox Identifiers CASNo 2381 08 0 PubChem 109 SMILES C C C O O N S O O MeSHName cysteine sulfinic acid Section2 Chembox Properties Formula C sub 3 sub H sub 7 sub NO sub 4 sub S MolarMass 153.15698 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Cysteine sulfinic acid is an intermediate in cysteine metabolism . It is formed by cysteine dioxygenase . Amino acid metabolism intermediates Category Sulfur amino acids Category Sulfinic acids organic compound stub fr Acide cyst ine sulfinique ja ... more details
enzyme Name D cysteine desulfhydrase EC number 4.4.1.15 CAS number 84012 74 8 IUBMB EC number 4 4 1 15 GO code 0019148 image width caption In enzymology , a D cysteine desulfhydrase EC number 4.4.1.15 is an enzyme that catalysis catalyzes the chemical reaction D cysteine H sub 2 sub O math rightleftharpoons math sulfide NH sub 3 sub pyruvate Thus, the two substrate biochemistry substrates of this enzyme are D cysteine and water H sub 2 sub O , whereas its 3 product chemistry products are sulfide , ammonia NH sub 3 sub , and pyruvate . This enzyme belongs to the family of lyase s, specifically the class of carbon sulfur lyases. The systematic name of this enzyme class is D cysteine sulfide lyase deaminating pyruvate forming . Other names in common use include D cysteine lyase , and D cysteine sulfide lyase deaminating . This enzyme participates in cysteine metabolism . References reflist 1 cite journal author Nagasawa T, Ishii T, Kumagai H, Yamada H date 1985 title D Cysteine desulfhydrase of Escherichia coli. Purification and characterization journal Eur. J. Biochem. volume 153 pages 541&ndash 51 pmid 3908101 doi 10.1111 j.1432 1033.1985.tb09335.x issue 3 cite journal author Schmidt A date 1982 title A cysteine desulfhydrase from spinach leaves specific for D cysteine journal Z. Pflanzenphysiol. volume 107 pages 301&ndash 312 cite journal author Schmidt A and Erdle I date 1983 title A cysteine desulfhydrase specific for D cysteine from the green alga Chlorella fusca journal Z. Naturforsch. C Biosci. volume 38 pages 428&ndash 435 lyase stub Category EC 4.4.1 Category Enzymes of unknown structure ... more details
enzyme Name cysteine S conjugate N acetyltransferase EC number 2.3.1.80 CAS number 81725 80 6 IUBMB EC number 2 3 1 80 GO code 0047198 image width caption In enzymology , a cysteine S conjugate N acetyltransferase EC number 2.3.1.80 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA an S substituted L cysteine math rightleftharpoons math CoA an S substituted N acetyl L cysteine Thus, the two substrate biochemistry substrates of this enzyme are acetyl CoA and S substituted L cysteine , whereas its two product chemistry products are coenzyme A CoA and S substituted N acetyl L cysteine . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl CoA S substituted L cysteine N acetyltransferase . This enzyme participates in glutathione metabolism . References reflist 1 cite journal author Duffel MW, Jakoby WB date 1982 title Cysteine S conjugate N acetyltransferase from rat kidney microsomes journal Mol. Pharmacol. volume 21 pages 444&ndash 8 pmid 6892478 issue 2 transferase stub Category EC 2.3.1 Category Enzymes of unknown structure it Cisteina S conjugato N acetiltransferasi ... more details
enzyme Name cysteine conjugate transaminase EC number 2.6.1.75 CAS number 117698 05 2 IUBMB EC number 2 6 1 75 GO code 0047802 image width caption In enzymology , a cysteine conjugate transaminase EC number 2.6.1.75 is an enzyme that catalysis catalyzes the chemical reaction S 4 bromophenyl L cysteine 2 oxoglutarate math rightleftharpoons math S 4 bromophenyl mercaptopyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are S 4 bromophenyl L cysteine and 2 oxoglutarate , whereas its two product chemistry products are S 4 bromophenyl mercaptopyruvate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is S 4 bromophenyl L cysteine 2 oxoglutarate aminotransferase . Other names in common use include cysteine conjugate aminotransferase , and cysteine conjugate alpha ketoglutarate transaminase CAT 1 . References reflist 1 cite journal author Tateishi M date 1988 title Purification and characterization of cysteine conjugate transaminases from rat liver journal Xenobiotica. volume 18 pages 1015&ndash 28 pmid 2852419 doi 10.3109 00498258809042224 last2 Ichimoto first2 N last3 Takanohashi first3 Y last4 Ichihara first4 S last5 Fukazawa first5 H last6 Tateishi first6 M issue 9 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
Encyclopedia
top
