1 17 4 1 GO code 0004748 image width caption Ribonucleotidereductase RNR, also known as ribonucleoside ... Eklund H, Eriksson M, Uhlin U, Nordlund P, Logan D title Ribonucleotidereductase structural studies ... Harnessing free radicals formation and function of the tyrosyl radical in ribonucleotidereductase ... . Structure The iron dependent enzyme, ribonucleotidereductase RNR , is essential for DNA synthesis ... 15.4 LocusSupplementaryData protein Name RRM2 ribonucleotidereductase M2 polypeptide caption image ... ribonucleotidereductase M2 B TP53 inducible caption image width HGNCid 17296 Symbol RRM2B AltSymbols ... top Pfam box Symbol RR N Name Ribonucleotidereductase br N terminal image 1PEU R1E.png width caption Crystallographic structure of the ribonucleotidereductase protein R1E from Salmonella typhimurium ... R, Eklund H, Uhlin U title Structure of the large subunit of class Ib ribonucleotidereductase ... reductase br all alpha domain image PDB 1rlr EBI.jpg width caption Structure of ribonucleotidereductase ... lgC Name Ribonucleotidereductase br barrel domain image PDB 1pem EBI.jpg width caption Structure of ribonucleotidereductase protein R1E from Salmonella typhimurium . ref name pmid12818204 cite journal ... subunit of class Ib ribonucleotidereductase from Salmonella typhimurium and its complexes with allosteric ... box Symbol Ribonuc red sm Name Ribonucleotidereductase br small chain image PDB 1rib EBI.jpg width caption Structure of the Escherichia coli ribonucleotidereductase protein R2. ref name pmid8331655 ... manganese centres in Mn substituted class I ribonucleotidereductase from Escherichia coli carboxylate ... 2002 cite journal author Pham DQ, Blachuta BJ, Nichol H, Winzerling JJ title Ribonucleotidereductase ... title Turning on ribonucleotidereductase by light initiated amino acid radical generation journal ... ribonucleotidereductase RNR catalyzes the de novo synthesis of dNTPs. ref name isbn0 7167 7108 X ... by enzyme ribonucleotidereductase understanding the role of the enzyme journal J Comput Chem ... more details
Ribonucleotidereductase inhibitors are a family of anti cancer drug s that interfere with the growth of tumor cells by blocking the formation of deoxyribonucleotides building blocks of DNA . Examples include motexafin gadolinium . ref name pmid19121624 Cite journal author Zahedi Avval F, Berndt C, Pramanik A, Holmgren A title Mechanism of inhibition of ribonucleotidereductase with motexafin gadolinium MGd journal Biochem. Biophys. Res. Commun. volume 379 issue 3 pages 775 9 year 2009 month January pmid 19121624 doi 10.1016 j.bbrc.2008.12.128 url http linkinghub.elsevier.com retrieve pii S0006 291X 08 02551 5 ref hydroxyurea ref name pmid12630679 Cite journal author Mayhew CN, Phillips JD, Cibull ML, Elford HL, Gallicchio VS title Short term treatment with novel ribonucleotidereductase inhibitors Trimidox and Didox reverses late stage murine retrovirus induced lymphoproliferative disease with less bone marrow toxicity than hydroxyurea journal Antivir. Chem. Chemother. volume 13 issue 5 pages 305 14 year 2002 month September pmid 12630679 doi url ref fludarabine , cladribine , gemcitabine , tezacitabine , and triapine ref name pmid12647987 Cite journal author Tsimberidou AM, Alvarado Y, Giles FJ title Evolving role of ribonucleoside reductase inhibitors in hematologic malignancies journal Expert Rev Anticancer Ther volume 2 issue 4 pages 437 48 year 2002 month August pmid 12647987 doi 10.1586 14737140.2.4.437 url http www.future drugs.com doi abs 10.1586 14737140.2.4.437?url ver Z39.88 2003&rfr id ori rid crossref.org&rfr dat cr pub 3dncbi.nlm.nih.gov ref gallium maltolate , gallium nitrate ref name PharmRev Cite journal author Bernstein LR title Mechanisms of therapeutic ... cgi reprint 50 4 665.pdf pmid 9860806 issue 4 ref See also Ribonucleotidereductase References Reflist External links http www.cancer.gov Templates db alpha.aspx?CdrID 349442 Ribonucleotidereductase inhibitor entry in the public domain NCI Dictionary of Cancer Terms NCI cancer dict ... more details
A ribonucleotide or ribotide is a nucleotide in which a purine or pyrimidine base is linked to a ribose molecule and exactly one phosphate group. ref cite book title The ACS style guide effective communication of scientific information year 2006 publisher American Chemical Society location Washington, D.C. isbn 9780841239999 edition 3rd editor Coghill, Anne M. Garson, Lorrin R. page 244 ref In living organisms the most common bases for ribonucleotides are adenine A , guanine G , cytosine C , or uracil U . See also Ribonucleosides or ribosides References reflist Nucleobases, nucleosides, and nucleotides Category RNA Category Ribosides Biochem stub de Ribonukleotide es Ribonucle tido fr Ribonucl otide it Ribonucleotide nl Ribonucleotide oc Ribonucleotid pl Rybonukleotydy ru sr Ribonukleotid ... more details
chembox verifiedrevid 280244659 ImageFile Glycineamide ribonucleotide.svg ImageSize IUPACName 2 R ,3 S ,4 R ,5 R 5 2 aminoacetyl amino 3,4 dihydroxyoxolan 2 yl methyldihydrogen phosphate OtherNames Glycineamide ribotide, br GAR Section1 Chembox Identifiers CASNo 10074 18 7 PubChem 160913 SMILES C C H 1 C H C H C H O1 NC O CN O O OP O O O MeSHName Glycineamide ribonucleotide Section2 Chembox Properties Formula C sub 7 sub H sub 15 sub N sub 2 sub O sub 8 sub P MolarMass 286.18 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Glycineamide ribonucleotide or GAR is an intermediate in the synthesis of purine s. organic compound stub Nucleotide metabolism intermediates Category Nucleotides ... more details
A reductase is an enzyme that Catalysis catalyzes a Redox reduction reaction . ref eMedicineDictionary Reductase ref ref DorlandsDict seven 000091316 Reductase ref Examples 5 alpha reductase Dihydrofolate reductase HMG CoA reductase Methemoglobin reductaseRibonucleotidereductase Thioredoxin reductase E. coli nitroreductase E. coli nitroreductase Methylenetetrahydrofolate reductase See also oxidase oxidoreductase References references enzymes Category Enzymes Enzyme stub fr R ductase ja pl Reduktazy ... more details
enzyme Name urate ribonucleotide phosphorylase EC number 2.4.2.16 CAS number 9030 29 9 IUBMB EC number 2 4 2 16 GO code 0050384 image width caption In enzymology , an urate ribonucleotide phosphorylase EC number 2.4.2.16 is an enzyme that catalysis catalyzes the chemical reaction urate D ribonucleotide phosphate math rightleftharpoons math urate alpha D ribose 1 phosphate Thus, the two substrate biochemistry substrates of this enzyme are urate D ribonucleotide and phosphate , whereas its two product chemistry products are urate and alpha D ribose 1 phosphate . This enzyme belongs to the family of glycosyltransferase s, specifically the pentosyltransferases. The systematic name of this enzyme class is urate ribonucleotide phosphate alpha D ribosyltransferase . Other names in common use include UAR phosphorylase , and urate ribonucleotide phosphate D ribosyltransferase . This enzyme participates in purine metabolism . References reflist 1 cite journal author Laster L and Blair A date 1963 title An intestinal phosphorylase for uric acid ribonucleoside journal J. Biol. Chem. volume 238 pages 3348&ndash 3357 pmid 14085385 enzyme stub Category EC 2.4.2 Category Enzymes of unknown structure ... more details
targets tumor cells, leading to cell death and apoptosis via inhibition of thioredoxin reductase and ribonucleotide ... and ribonucleotidereductase journal J. Biol. Chem. volume 281 issue 16 pages 10691 10697 year ...enzyme Name Thioredoxin disulfide reductase EC number 1.8.1.9 CAS number 9074 14 0 IUBMB EC number 1 8 1 9 GO code 0004791 image TrxR.png width caption Crystal structure of human TXNRD1 thioredoxin reductase ... G title Thioredoxin reductase journal Biochem. J. volume 346 issue Pt 1 pages 1 8 year 2000 month February pmid 10657232 pmc 1220815 doi 10.1042 0264 6021 3460001 ref Two classes of thioredoxin reductase ... reductase new perspectives journal Trends Parasitol. volume 18 issue 7 pages 302 8 year 2002 month July pmid 12379950 doi 10.1016 S1471 4922 02 02293 6 url ref Cellular Role Thioredoxin reductase ... Lu title Thioredoxin and thioredoxin reductase Current research with special reference to human ... reductase have evolved independently A high molecular weight MW 55,000 type containing a selenocysteine ... is related to glutathione reductase , trypanothione disulfide reductase trypanothione reductase , mercuric reductase and dihydrolipoamide dehydrogenase lipoamide dehydrogenase . ref name Hirt 2002 A low ... author Arscott LD, Gromer S, Schirmer RH, Becker K, Williams CH title The mechanism of thioredoxin reductase ... reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli journal ... 20490 doi 10.1073 pnas.94.8.3621 ref Humans express three thioredoxin reductase isozymes TrxR1 cytosolic ... thioredoxin reductase in hematopoiesis, heart development, and heart function journal Mol. Cell. Biol ... 522221 ref Each isozyme is encoded by a separate gene protein Name TXNRD1 thioredoxin reductase 1 ... thioredoxin reductase 2 caption image width HGNCid 18155 Symbol TXNRD2 AltSymbols EntrezGene 10587 ... protein Name thioredoxin reductase 3 caption image width HGNCid 20667 Symbol TXNRD3 ... Chromosome 3 Arm p Band 13 LocusSupplementaryData q13.33 Structure E. coli thioredoxin reductase structure ... more details
enzyme Name flavin reductase EC number 1.5.1.30 CAS number 56626 29 0 IUBMB EC number 1 5 1 30 GO code 0042602 image width caption In enzymology , a flavin reductase EC number 1.5.1.30 is an enzyme that catalysis catalyzes the chemical reaction reduced riboflavin NADP sup sup math rightleftharpoons math riboflavin NADPH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are reduced riboflavin and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 3 product chemistry products are riboflavin , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with NAD sup sup or NADP sup sup as acceptor. The systematic name of this enzyme class is reduced riboflavin NADP oxidoreductase . Other names in common use include NADPH flavin oxidoreductase , riboflavin mononucleotide reduced nicotinamide adenine dinucleotide , phosphate reductase , flavin mononucleotide reductase , flavine mononucleotide reductase , FMN reductase NADPH , NADPH dependent FMN reductase , NADPH flavin reductase , NADPH FMN reductase , NADPH specific FMN reductase , riboflavin mononucleotide reductase , riboflavine mononucleotide reductase , NADPH2 dehydrogenase flavin , and NADPH2 riboflavin oxidoreductase . References reflist 1 cite journal author Lo H, Reeves RE date 1980 title Purification and properties of NADPH flavin oxidoreductase from Entamoeba histolytica journal Mol. Biochem. Parasitol. volume 2 pages 23&ndash 30 pmid 6258069 doi 10.1016 0166 6851 80 90045 6 issue 1 cite journal author Yubisui T, Tamura M, Takeshita M date 1987 title Characterization of a second form of NADPH flavin reductase purified from human erythrocytes journal Biochem. Int. volume 15 pages 1&ndash 8 pmid 3453680 issue 1 1.5 enzyme stub Category EC 1.5.1 Category NADPH dependent enzymes Category Enzymes of unknown structure it Flavina reduttasi ja ... more details
DMSO reductase is a molybdenum containing enzyme capable of reducing dimethyl sulfoxide DMSO to dimethyl sulfide DMS . This enzyme serves as the terminal Oxidoreductase reductase under anaerobic conditions in some bacteria, with DMSO being the terminal electron acceptor. During the course of the reaction, the oxygen atom in DMSO is transferred to molybdenum, and then is subsequently removed from molybdenum as water. Image DMSO reductase reaction.png thumb 500px none The reaction catalyzed by DMSO reductase. Active site and mechanism The active site contains a molybdopterin containing core that supports molybdenum in its highest oxidation state Mo sup VI sup . The proposed mechanism of DMSO reductase cycles molybdenum between the 4 and 6 oxidation states. Image DMSO reductase mechanism.png thumb 500px none The proposed mechanism of DMSO reductase. References cite journal author Kisker, C. Schindelin, H. Baas, D. R tey, J. Meckenstock, R.U. Kroneck, P.M.H. title A structural comparison of molybdenum cofactor containing enzymes journal FEMS Microbiol. Rev. year 1999 volume 22 pages 503 521 doi 10.1111 j.1574 6976.1998.tb00384.x pmid 9990727 issue 5 PMID 9990727 Category Oxidoreductases Category Metalloproteins Category Molybdenum compounds ... more details
Pfam box Symbol Fum red TM Name Fumarate reductase respiratory complex image PDB 2bs3 EBI.jpg width caption Structure of Quinol Fumarate Reductase Flavoprotein Subunit A. ref name pmid16380425 cite journal author Lancaster CR, Sauer US, Gross R, et al. title Experimental support for the E pathway hypothesis of coupled transmembrane e and H transfer in dihemic quinol fumarate reductase journal Proc. Natl. Acad. Sci. U.S.A. volume 102 issue 52 pages 18860 5 year 2005 month December pmid 16380425 pmc 1323215 doi 10.1073 pnas.0509711102 url ref Pfam PF01127 Pfam clan CL0335 InterPro IPR004224 SMART PROSITE SCOP 1qla TCDB OPM family 3 OPM protein 2bs3 PDB PDB3 1qla F 1 243 PDB3 2bs3 F 1 243 PDB3 1qlb C 1 243 PDB3 2bs4 F 1 243 Infobox protein family Symbol Fumarate red C Name Fumarate reductase subunit C image PDB 1l0v EBI.jpg width caption quinol fumarate reductase with menaquinol molecules Pfam ... CAZy CDD Infobox protein family Symbol Fumarate red D Name Fumarate reductase subunit D image PDB 1kfy EBI.jpg width caption quinol fumarate reductase with quinol inhibitor 2 1 4 chloro phenyl ethyl ... TCDB OPM family OPM protein CAZy CDD Fumarate reductase is the enzyme that converts fumaric acid ... of the Escherichia coli fumarate reductase respiratory complex journal Science volume 284 issue ... reduced acceptor In other words, fumarate reductase couples the reduction of fumarate to succinate ... Michel H, Lancaster CR, Kroger A, Auer M title Structure of fumarate reductase from Wolinella ... doi 10.1038 45133 ref Fumarate reductase complex includes three subunits. Subunit A contains ... subunit may be required to anchor the catalysis catalytic components of the fumarate reductase ... 2 External links http prosite.expasy.org PDOC00393 Fumarate reductase succinate dehydrogenase FAD binding site in PROSITE MeshName Fumarate Reductase EC number 1.3.99.1 CH CH oxidoreductases InterPro content IPR004224 InterPro content IPR003510 InterPro content IPR003418 DEFAULTSORT Fumarate Reductase ... more details
Merge to 6,7 dihydropteridine reductase discuss Talk 6,7 dihydropteridine reductase Merge discussion date March 2011 Dihydrobiopterin is a compound produced in the synthesis of dopamine , norepinephrine and epinephrine through production of the intermediate 3,4 dihydroxy phenylalanine, also known as dopa . Phenylalanine is converted into dopa using tetrahydrobiopterin releasing dihydrobiopterin and water, which is then converted back into tetrahydrobiopterin using the NADPH dependent enzyme dihydrobiopterin reductase. This enzyme is sometimes defective in patients with phenylketonuria , and is treated in the same fashion, with tyrosine supplements and a controlled diet which is lacking in phenylalanine . ref cite book author Pawlina, Wojciech Ross, Michael W. title Histology a text and atlas with correlated cell and molecular biology publisher Lippincott Wiliams & Wilkins location Philadelphia year 2006 pages isbn 0 7817 5056 3 ref See also Sepiapterin reductase References reflist Category Biochemistry Category EC 1.5.1 ... more details
enzyme Name cystine reductase EC number 1.8.1.6 CAS number 9029 18 9 IUBMB EC number 1 8 1 6 GO code 0050456 image width caption In enzymology , a cystine reductase EC number 1.8.1.6 is an enzyme that catalysis catalyzes the chemical reaction 2 L cysteine NAD sup sup math rightleftharpoons math L cystine NADH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are L cysteine and nicotinamide adenine dinucleotide NAD sup sup , whereas its 3 product chemistry products are L cystine , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on a sulfur group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is L cysteine NAD oxidoreductase . Other names in common use include cystine reductase NADH , NADH dependent cystine reductase , cystine reductase NADH2 , and NADH2 L cystine oxidoreductase . This enzyme participates in cysteine metabolism . References reflist 1 cite journal author ROMANO AH, NICKERSON WJ date 1954 title Cystine reductase of pea seeds and yeasts journal J. Biol. Chem. volume 208 pages 409&ndash 16 pmid 13174550 issue 1 cite journal author Carroll JE, Kosicki GW, Thibert RJ date 1970 title Alpha substituted cystines as possible substrates for cystine reductase and L amino acid oxidase journal Biochim. Biophys. Acta. volume 198 pages 601&ndash 3 pmid 5436160 issue 3 cite journal author Maresca B, Jacobson E, Medoff G, Kobayashi G date 1978 title Cystine reductase in the dimorphic fungus Histoplasma capsulatum journal J. Bacteriol. volume 135 pages 987&ndash 92 pmid 211119 issue 3 pmc 222474 1.8 enzyme stub Category EC 1.8.1 Category NADH dependent enzymes Category Enzymes of unknown structure it Cistina reduttasi ja ... more details
Merge from Dihydrobiopterin reductase discuss Talk 6,7 dihydropteridine reductase Merge discussion date March 2011 enzyme Name 6,7 dihydropteridine reductase EC number 1.5.1.34 CAS number 9074 11 7 IUBMB EC number 1 5 1 34 GO code 0004155 image width caption In enzymology , a 6,7 dihydropteridine reductase EC number 1.5.1.34 is an enzyme that catalysis catalyzes the chemical reaction a 5,6,7,8 tetrahydropteridine NAD P math rightleftharpoons math a 6,7 dihydropteridine NAD P H H sup sup The 3 substrate biochemistry substrates of this enzyme are 5,6,7,8 tetrahydropteridine , nicotinamide adenine dinucleotide NAD sup sup , and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 4 product chemistry products are 6,7 dihydropteridine , nicotinamide adenine dinucleotide NADH , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is 5,6,7,8 tetrahydropteridine NAD P oxidoreductase . Other names in common use include 6,7 dihydropteridine NAD P H oxidoreductase , DHPR , NAD P H 6,7 dihydropteridine oxidoreductase , NADH dihydropteridine reductase , NADPH dihydropteridine reductase , NADPH specific dihydropteridine reductase , dihydropteridine reduced nicotinamide adenine dinucleotide , reductase , dihydropteridine reductase , dihydropteridine reductase NADH , and 5,6,7,8 tetrahydropteridine NAD P H oxidoreductase . This enzyme participates in folate biosynthesis ... silkworm eggs. NADH NADPH cytochrome c reductase activity mediated with 6,7 dimethyltetrahydropterin ... cite journal author Hasegawa H date Tokyo title Dihydropteridine reductase from bovine liver. Purification ... reductase. Investigation of the specificity for quinoid dihydropteridine and the inhibition ... Tokyo title A new enzyme, NADPH dihydropteridine reductase in bovine liver journal J. volume Biochem ... more details
enzyme Name dTDP 4 dehydrorhamnose reductase EC number 1.1.1.133 CAS number 37250 64 9 IUBMB EC number 1 1 1 133 GO code 0008831 image width caption In enzymology , a dTDP 4 dehydrorhamnose reductase EC number 1.1.1.133 is an enzyme that catalysis catalyzes the chemical reaction dTDP 6 deoxy L mannose NADP sup sup math rightleftharpoons math dTDP 4 dehydro 6 deoxy L mannose NADPH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are dTDP 6 deoxy L mannose and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 3 product chemistry products are dTDP 4 dehydro 6 deoxy L mannose , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is dTDP 6 deoxy L mannose NADP 4 oxidoreductase . Other names in common use include dTDP 4 keto L rhamnose reductase , reductase, thymidine diphospho 4 ketorhamnose , dTDP 4 ketorhamnose reductase , TDP 4 keto rhamnose reductase , and thymidine diphospho 4 ketorhamnose reductase . This enzyme participates in 3 metabolism metabolic pathways nucleotide sugars metabolism , streptomycin biosynthesis , and polyketide sugar unit biosynthesis . Structural studies As of late 2007, 5 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1KBZ , PDB link 1KC1 , PDB link 1KC3 , PDB link 1N2S , and PDB link 2GGS . References reflist 1 cite journal author Melo A, Glaser L date 1968 title The mechanism of 6 deoxyhexose synthesis. II. Conversion of deoxythymidine diphosphate 4 keto 6 deoxy D glucose to deoxythymidine diphosphate L rhamnose journal J. Biol. Chem. volume 243 pages 1475&ndash 8 pmid 4384782 issue 7 1.1.1 enzyme stub Category EC 1.1.1 Category NADPH dependent enzymes Category Enzymes of known structure it dTDP 4 deidroramnosio reduttasi ... more details
enzyme Name glyoxylate reductase EC number 1.1.1.26 CAS number 9028 32 4 IUBMB EC number 1 1 1 26 GO code 0047964 image width caption In enzymology , a glyoxylate reductase EC number 1.1.1.26 is an enzyme that catalysis catalyzes the chemical reaction glycolate NAD sup sup math rightleftharpoons math glyoxylate NADH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are glycolate and nicotinamide adenine dinucleotide NAD sup sup , whereas its 3 product chemistry products are glyoxylate , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is glycolate NAD oxidoreductase . Other names in common use include NADH glyoxylate reductase , glyoxylic acid reductase , and NADH dependent glyoxylate reductase . This enzyme participates in glyoxylate and dicarboxylate metabolism . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2DBQ , PDB link 2DBR , and PDB link 2DBZ . References reflist 1 cite journal author Zelitch I year 1953 title Oxidation and reduction of glycolic and glyoxylic acids in plants II. Glyoxylic acid reductase journal J. Biol. Chem. volume 201 pages 719&ndash 726 pmid 13061410 issue 2 cite journal author Zelitch I year 1955 title The isolation and action of crystalline glyoxylic acid reductase from tobacco leaves journal J. Biol. Chem. volume 216 pages 553&ndash 575 pmid 13271335 issue 2 Category EC 1.1.1 Category NADH dependent enzymes Category Enzymes of known structure 1.1.1 enzyme stub it Gliossilato reduttasi ja ... more details
enzyme Name chlorate reductase EC number 1.97.1.1 CAS number 60382 73 2 IUBMB EC number 1 97 1 1 GO code 0047143 image width caption In enzymology , a chlorate reductase EC number 1.97.1.1 is an enzyme that catalysis catalyzes the chemical reaction AH sub 2 sub chlorate math rightleftharpoons math A H sub 2 sub O chlorite Thus, the two substrate biochemistry substrates of this enzyme are AH sub 2 sub and chlorate , whereas its 3 product chemistry products are A, water H sub 2 sub O , and chlorite . This enzyme belongs to the family of oxidoreductase s. The systematic name of this enzyme class is chlorite acceptor oxidoreductase . This enzyme is also called chlorate reductase C . References reflist 1 cite journal author Azoulay E, Mutaftschiev S, Martins Rosado de Sousa date 1971 title Study of chlorate resistant mutants in Escherichia coli K 12. 3 Chlorate reductase c of mutants chl. C journal Biochim. Biophys. Acta. volume 237 pages 579&ndash 90 pmid 4940765 issue 3 1.97 enzyme stub Category EC 1.97.1 Category Enzymes of unknown structure it Clorato reduttasi ja ... more details
enzyme Name methylarsonate reductase EC number 1.20.4.2 CAS number IUBMB EC number 1 20 4 2 GO code 0050610 image width caption In enzymology , a methylarsonate reductase EC number 1.20.4.2 is an enzyme that catalysis catalyzes the chemical reaction methylarsonate 2 glutathione math rightleftharpoons math methylarsonite glutathione disulfide H sub 2 sub O Thus, the two substrate biochemistry substrates of this enzyme are methylarsonate and glutathione , whereas its 3 product chemistry products are methylarsonite , glutathione disulfide , and water H sub 2 sub O . This enzyme belongs to the family of oxidoreductase s, specifically those acting on phosphorus or arsenic in donor with disulfide as acceptor. The systematic name of this enzyme class is gluthathione methylarsonate oxidoreductase . This enzyme is also called MMA V reductase . References reflist 1 cite journal author Zakharyan RA, Aposhian HV date 1999 title Enzymatic reduction of arsenic compounds in mammalian systems the rate limiting enzyme of rabbit liver arsenic biotransformation is MMA V reductase journal Chem. Res. Toxicol. volume 12 pages 1278&ndash 83 pmid 10604879 doi 10.1021 tx9901231 issue 12 1.20 enzyme stub Category EC 1.20.4 Category Enzymes of unknown structure it Metilarsonato reduttasi ja ... more details
enzyme Name Vinylphenol reductase EC number CAS number IUBMB EC number GO code image width caption Vinylphenol reductase is an enzyme that catalyses the reaction 4 vinylphenol Nicotinamide adenine dinucleotide NAD sup sup 3 H sup sup 4 ethylphenol NADH It is found in Brettanomyces bruxellensis ref Partial vinylphenol reductase purification and characterization from Brettanomyces bruxellensis. Iavor Tchobanov, Laurent Gal, Mich le Guilloux Benatier, Fabienne Remize, Tiziana Nardi, Jean Guzzo, Virginie Serpaggi and Herv Alexandre, FEMS Microbiology Letters, Volume 284, Issue 2, pages 213 217, July 2008, doi 10.1111 j.1574 6968.2008.01192.x ref , a yeast responsible of the presence of ethyl phenols in wine formed from p coumaric acid . ref The origin of ethylphenols in wines. Pascal Chatonnet, Denis Dubourdie, Jean no l Boidron and Monique Pons, Journal of the Science of Food and Agriculture, Volume 60, Issue 2, pages 165 178, 1992, doi 10.1002 jsfa.2740600205 ref See also Wine chemistry References reflist External links http biocyc.org META NEW IMAGE?type ENZYME&object MONOMER 14367 Vinylphenol reductase on MetaCyc Category Oxidoreductases enzyme stub ... more details
protein Name guanosine monophosphate reductase caption image width HGNCid 4376 Symbol GMPR AltSymbols EntrezGene 2766 OMIM 139265 RefSeq NM 006877 UniProt P36959 PDB ECnumber 1.7.1.7 Chromosome 6 Arm p Band 23 LocusSupplementaryData protein Name guanosine monophosphate reductase 2 caption image width HGNCid 4377 Symbol GMPR2 AltSymbols EntrezGene 51292 OMIM 610781 RefSeq NM 016576 UniProt Q9P2T1 PDB ECnumber Chromosome 14 Arm q Band 11.2 LocusSupplementaryData GMP reductase EC number 1.7.1.7 Guanosine 5 monophosphate oxidoreductase is an enzyme that catalyses the irreversible and NADPH dependent reductive deamination of Guanosine monophosphate GMP into Inosine monophosphate IMP . ref name pmid2904262 cite journal author Andrews SC, Guest JR title Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12 journal Biochem. J. volume 255 issue 1 pages 35 43 year 1988 month October pmid 2904262 pmc 1135187 doi url ref NADPH Guanosine monophosphate guanosine 5 phosphate NADP sup sup Inosine monophosphate inosine 5 phosphate NH sub 3 sub It converts nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and maintains intracellular balance of A and G nucleotide nucleotides . In melanocytic cells, GMP reductase gene expression may be regulated by Microphthalmia associated transcription factor MITF . ref name pmid19067971 cite journal author Hoek KS, Schlegel NC, Eichhoff OM, et al. title Novel MITF targets identified using a two step DNA microarray strategy journal Pigment Cell Melanoma Res. volume 21 issue 6 pages 665 76 year 2008 pmid 19067971 doi 10.1111 j.1755 148X.2008.00505.x issn ref See also Purine metabolism References reflist External links MeshName GMP reductase Nitrogenous donor oxidoreductases Nucleotide metabolism InterPro content IPR001093 biochemistry stub it GMP reduttasi ja GMP ... more details
enzyme Name 2 oxoadipate reductase EC number 1.1.1.172 CAS number 61116 21 0 IUBMB EC number 1 1 1 172 GO code 0047550 image width caption In enzymology , a 2 oxoadipate reductase EC number 1.1.1.172 is an enzyme that catalysis catalyzes the chemical reaction 2 hydroxyadipate NAD sup sup math rightleftharpoons math 2 oxoadipate NADH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are 2 hydroxyadipate and nicotinamide adenine dinucleotide NAD sup sup , whereas its 3 product chemistry products are 2 oxoadipate , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is 2 hydroxyadipate NAD 2 oxidoreductase . Other names in common use include 2 ketoadipate reductase , alpha ketoadipate reductase , and 2 ketoadipate reductase . References reflist 1 cite journal author Suda T, Robinson JC, Fjellstedt TA date 1976 title Purification and properties of alpha ketoadipate reductase, a newly discovered enzyme from human placenta journal Arch. Biochem. Biophys. volume 176 pages 610&ndash 20 pmid 185965 doi 10.1016 0003 9861 76 90205 8 issue 2 1.1.1 enzyme stub Category EC 1.1.1 Category NADH dependent enzymes Category Enzymes of unknown structure it 2 ossoadipato reduttasi ja 2 ... more details
enzyme Name aquacobalamin reductase EC number 1.16.1.3 CAS number 37256 39 6 IUBMB EC number 1 16 1 3 GO code 0047138 image width caption In enzymology , an aquacobalamin reductase EC number 1.16.1.3 is an enzyme that catalysis catalyzes the chemical reaction 2 cob II alamin NAD sup sup math rightleftharpoons math 2 aquacob III alamin NADH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are cob II alamin and nicotinamide adenine dinucleotide NAD sup sup , whereas its 3 product chemistry products are aquacob III alamin , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those oxidizing metal ion with NAD or NADP as acceptor. The systematic name of this enzyme class is cob II alamin NAD oxidoreductase . Other names in common use include aquocobalamin reductase , vitamin B12a reductase , NADH linked aquacobalamin reductase , B12a reductase , and NADH2 cob III alamin oxidoreductase . This enzyme participates in porphyrin and chlorophyll metabolism . It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author Walker GA, Murphy S, Huennekens FM date 1969 title Enzymatic conversion of vitamin B 12a to adenosyl B 12 evidence for the existence of two separate reducing systems journal Arch. Biochem. Biophys. volume 134 pages 95&ndash 102 pmid 4390543 doi 10.1016 0003 9861 69 90255 0 issue 1 1.16 enzyme stub Category EC 1.16.1 Category NADH dependent enzymes Category Flavin enzymes Category Enzymes of unknown structure it Acquacobalamina reduttasi ja ... more details
enzyme Name delta1 piperideine 2 carboxylate reductase EC number 1.5.1.21 CAS number 52037 88 4 IUBMB EC number 1 5 1 21 GO code 0047125 image width caption In enzymology , a Delta1 piperideine 2 carboxylate reductase EC number 1.5.1.21 is an enzyme that catalysis catalyzes the chemical reaction L pipecolate NADP sup sup math rightleftharpoons math Delta sub 1 sub piperideine 2 carboxylate NADPH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are L pipecolate and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 3 product chemistry products are Delta1 piperideine 2 carboxylate , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is L pipecolate NADP 2 oxidoreductase . Other names in common use include 1,2 didehydropipecolate reductase , P2C reductase , and 1,2 didehydropipecolic reductase . This enzyme participates in lysine degradation . References reflist 1 cite journal author Payton CW, Chang YF date 1982 title delta1 piperideine 2 carboxylate reductase of Pseudomonas putida journal J. Bacteriol. volume 149 pages 864&ndash 71 pmid 6801013 issue 3 pmc 216472 1.5 enzyme stub Category EC 1.5.1 Category NADPH dependent enzymes Category Enzymes of unknown structure it Delta1 piperideina 2 carbossilato reduttasi ja 1 2 ... more details
enzyme Name 2,5 didehydrogluconate reductase EC number 1.1.1.274 CAS number 95725 95 4 IUBMB EC number 1 1 1 274 GO code 0050580 image width caption In enzymology , a 2,5 didehydrogluconate reductase EC number 1.1.1.274 is an enzyme that catalysis catalyzes the chemical reaction 2 dehydro D gluconate NADP sup sup math rightleftharpoons math 2,5 didehydro D gluconate NADPH H sup sup Thus, the two substrate biochemistry substrates of this enzyme are 2 dehydro D gluconate and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 3 product chemistry products are 2,5 didehydro D gluconate , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is 2 dehydro D gluconate NADP 2 oxidoreductase . Other names in common use include 2,5 diketo D gluconate reductase , and YqhE reductase . 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 1VP5 . References reflist 1 cite journal author Yum DY, Lee BY, Pan JG date 1999 title Identification of the yqhE and yafB genes encoding two 2, 5 diketo D gluconate reductases in Escherichia coli journal Appl. Environ. Microbiol. volume 65 pages 3341&ndash 6 pmid 10427017 issue 8 pmc 91502 cite journal author Yum DY, Lee BY, Hahm DH, Pan JG date 1998 title The yiaE gene, located at 80.1 minutes on the Escherichia coli chromosome, encodes a 2 ketoaldonate reductase journal J. Bacteriol. volume 180 pages 5984&ndash 8 pmid 9811658 issue 22 pmc 107674 cite journal author Habrych M, Rodriguez S, Stewart JD date 2002 title Purification and identification of an Escherichia coli beta keto ester reductase as 2,5 diketo D gluconate reductase YqhE journal Biotechnol. Prog. volume 18 pages 257&ndash 61 pmid 11934293 doi ... more details
enzyme Name coenzyme F420 dependent N5,N10 methenyltetrahydromethanopterin reductase EC number 1.5.99.11 CAS number IUBMB EC number 1 5 99 11 GO code 0018537 image width caption In enzymology , a 5,10 methylenetetrahydromethanopterin reductase EC number 1.5.99.11 is an enzyme that catalysis catalyzes the chemical reaction 5 methyltetrahydromethanopterin coenzyme F sub 4 sub 20 math rightleftharpoons math 5,10 methylenetetrahydromethanopterin reduced coenzyme F sub 4 sub 20 Thus, the two substrate biochemistry substrates of this enzyme are 5 methyltetrahydromethanopterin and coenzyme F420 , whereas its two product chemistry products are 5,10 methylenetetrahydromethanopterin and reduced coenzyme F420. This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with other acceptors. The systematic name of this enzyme class is 5 methyltetrahydromethanopterin coenzyme F420 oxidoreductase . Other names in common use include 5,10 methylenetetrahydromethanopterin cyclohydrolase , N5,N10 methylenetetrahydromethanopterin reductase , methylene H4MPT reductase , coenzyme F420 dependent N5,N10 methenyltetrahydromethanopterin , reductase , and N5,N10 methylenetetrahydromethanopterin coenzyme F420 oxidoreductase . This enzyme participates in folate biosynthesis . 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 1Z69 . References reflist 1 cite journal author Ma K, Thauer RK year 1990 title Purification and properties of N5, N10 methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum strain ... dehydrogenase and 5,10 methylenetetrahydromethanopterin reductase, two ... Ma K, Thauer RK year 1990 title Single step purification of methylenetetrahydromethanopterin reductase ... reductase, a coenzyme F420 dependent enzyme, from Methanobacterium thermoautotrophicum strain ... more details
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