enzyme Name xyloseisomerase EC number 5.3.1.5 CAS number 9023 82 9 IUBMB EC number 5 3 1 5 GO code 0009045 image width caption In enzymology , a xyloseisomerase EC number 5.3.1.5 is an enzyme that catalysis catalyzes the chemical reaction D xylose math rightleftharpoons math D xylulose This enzyme belongs to the family of isomerase s, specifically those intramolecular oxidoreductase s interconverting aldose s and ketose s. The systematic name of this enzyme class is D xylose aldose ketose isomerase . Other names in common use include D xyloseisomerase , D xylose ketoisomerase , and D xylose ketol isomerase . This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism. The enzyme is used industrially to convert glucose to fructose in the manufacture of high fructose corn syrup . It is sometimes referred to as glucose isomerase . Structural studies As of late 2007, 73 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1A0C , PDB link 1A0D , PDB link 1A0E , PDB link 1BHW , PDB link 1BXB , PDB link 1BXC , PDB link 1CLK , PDB link 1DID , PDB link 1DIE , PDB link 1DXI , PDB link 1GW9 , PDB link 1MNZ , PDB link 1MUW , PDB link 1O1H , PDB link 1OAD , PDB link 1QT1 , PDB link 1S5M , PDB link 1S5N , PDB link 1XIA , PDB link 1XIB , PDB link 1XIC , PDB link 1XID , PDB link 1XIE , PDB link 1XIF , PDB link 1XIG , PDB link 1XIH , PDB link 1XII , PDB link 1XIJ , PDB link 1XIM , PDB link 1XIN , PDB link 1XIS , PDB link 1XLA , PDB link 1XLB , PDB link 1XLC , PDB link 1XLD ... Xyloseisomerase from Pasteurella pestis, strain A 1122 journal J. Am. Chem. Soc. volume 77 pages ..., crystallization and properties of the D xyloseisomerase from Lactobacillus brevis journal Biochim. Biophys. Acta. volume 151 pages 670&ndash 80 pmid 5646045 issue 3 isomerase stub Category ... isomerization of D xylose to D xylulose journal Arch. Biochem. Biophys. volume 48 pages 120&ndash ... more details
chembox Verifiedfields changed Watchedfields changed verifiedrevid 458276050 Name small D small Xylose ImageFileL1 Xylose.png ImageSizeL1 120px ImageNameL1 D Xylopyranose ImageFileR1 Xylofuranose.png ImageSizeR1 130px ImageNameR1 Xylofuranose ImageFile2 D Xylose.svg ImageSize2 180px ImageName2 Xylose chair ImageFile3 Xylose linear.png ImageSize3 180px ImageName3 Xylose linear IUPACName small D small Xylose OtherNames Xylose br Wood sugar Section1 Chembox Identifiers CASNo 58 86 6 CASNo Ref cascite correct CAS CASNo1 609 06 3 CASNo1 Comment small L small isomer CASNo1 Ref cascite correct ESIS CASNo2 ... Xylulose Xylose cf. Ancient Greek language Greek , xylos , wood is a sugar first isolated from wood, and named for it. Xylose is classified as a monosaccharide of the aldopentose type, which ... The acyclic form of xylose has chemical formula HOCH sub 2 sub carbon C H OH sub 3 sub CHO ..., depending on the relative orientation of the anomeric hydroxy group. Occurrence Xylose is the main building block for hemicellulose , which comprises about 30 of plant matter. Xylose is otherwise pervasive ... in 1881. Xylose is also the first saccharide added to the serine or threonine in the proteoglycan ... 119.pub2 ref Xylose is not metabolised by humans. It is completely absorbed and secreted from the kidneys. In animal medicine, xylose is used to test for malabsorption by administration in water to the patient after fasting . If xylose is detected in blood and or urine within the next few ... article 003606.htm title D xylose absorption work MedlinePlus publisher U.S. National Library of Medicine date July 2008 accessdate 2009 09 06 . ref Organic redox reaction Reduction of xylose by catalytic hydrogenation produces the non cariogenic sugar substitute xylitol . See also Xylose metabolism ... ca Xilosa da Xylose de Xylose es Xilosa eu Xilosa fr Xylose fy Ksyloaze gl Xilosa id Xilosa it D xilosio hu Xil z nl Xylose ja nn Xylose pl Ksyloza pt Xilose ru sr Ksiloza fi Ksyloosi ... more details
In biochemistry , an isomerase is an enzyme that catalyzes the structural rearrangement of isomer s. Isomerases thus catalyze reactions of the form A &rarr B where B is an isomer of A. Nomenclature The names of isomerases are formed as substrate isomerase for example, enoyl CoA isomerase , or as substrate type of isomerase for example, phosphoglucomutase . Classification Isomerases have their own Enzyme Commission number EC classification of enzymes EC 5 . Isomerases can be further classified into six subclasses Category EC 5.1 EC 5.1 includes enzymes that catalyze racemization racemase s and epimer ization epimerase s Category EC 5.2 EC 5.2 includes enzymes that catalyze the isomerization of geometric isomerism geometric isomers cis trans isomerase s Category EC 5.3 EC 5.3 includes intramolecular oxidoreductase s Category EC 5.4 EC 5.4 includes intramolecular transferase s mutase s Category EC 5.5 EC 5.5 includes intramolecular lyase s Category EC 5.99 EC 5.99 includes other isomerases including topoisomerase s References http www.chem.qmul.ac.uk iubmb enzyme EC5 intro.html EC 5 Introduction from the Department of Chemistry at Queen Mary, University of London isomerase. Dorland s Medical Dictionary for Health Consumers. 2007. Saunders, an imprint of Elsevier, Inc 6 Nov. 2009 http medical dictionary.thefreedictionary.com isomeraseisomerase. Webster s New World College Dictionary. LoveToKnow, n.d. Web. 6 November 2009. http www.yourdictionary.com isomerase External links http www.gopubmed.org GoMeshPubMed gomeshpubmed ?tool HotTopicDirect&termAlt mesh 237535 GoPubMed Top authors, journals, places publishing on Isomerases Enzymes Isomerases Category Isomerases ar bs Izomeraza bg ca Isomerasa cs Izomer za da Isomerase de Isomerasen es Isomerasa fa fr Isom rase gl Isomerase it Isomerasi he lt Izomeraz s nl Isomerase ja pl Izomerazy pt Isomerase ru sv Isomeras tr zomeraz zh ... more details
in an overproduction of xylitol byproduct. The isomerase pathway In this pathway the enzyme xyloseisomerase is responsible for the conversion of D xylose into D xylulose. D xylulose is then phosphorylated ... xyloseisomerase was introduced. Studies on flux through the pentose phosphate pathway during D xylose ... production. ref Karhumaa et al. , Comparison of the xylose reductase xylitol dehydrogenase and the xyloseisomerase pathways for xylose fermentation by recombinant Saccharomyces cerevisiae. Microbial ...File Xylose.png thumb Xylose D Xylose is a five carbon aldose pentose , monosaccharide that can be catabolized ... pathways for the catabolism of D xylose An oxireductive pathway that is present in eukaryotic microorganisms, an isomerase pathway, and two oxidative pathways that are called Weimberg and Dahms ... called the Xylose Reductase Xylitol Dehydrogenase or XR XDH pathway. Xylose reductase XR and xylitol dehydrogenase XDH are the first two enzymes in this pathway. XR is reducing D xylose to xylitol ... is an oxidative pathway where the D xylose is oxidized to D xylono lactone by a D xylose dehydrogenase ... of D xylose degradation. Biochem Biophys Res Commun. 60 1433 1439 ref starts as the Weimberg pathway ... applications It is desirable to ferment D xylose to ethanol however microorganisms that are naturally able to do that have disadvantages. One organism that can naturally ferment D xylose to ethanol ... D xylose to ethanol. In attempts to generate S.cerevisiae strains that are able to ferment D xylose ... A, Christensson C, Wahlbom CF, Hahn H gerdal B title Anaerobic xylose fermentation by recombinant Saccharomyces ... production include a lowering phosphoglucose isomerase activity, b deleting the GND1 gene, and c ... Xylose Utilizing Saccharomyces cerevisiae Strains Improves the Ethanol Yield from Xylose ... D xylose metabolizing pathways revealed that the XI pathway was best able to metabolize D xylose ... a yeast strain that efficiently produces ethanol. However, the effectiveness of D xylose metabolizing ... more details
Distinguish D xyloseisomerase enzyme Name Glucose 6 phosphate isomerase EC number 5.3.1.9 CAS number 9001 41 6 IUBMB EC number 5 3 1 9 GO code 0004347 image Glucose 6 phosphate isomerase 1GZV wpmp.png width caption Infobox protein family Symbol bact PGI C Name Bacterial phospho glucose isomerase C terminal ... isomerase from pyrobaculum aerophilum in complex with fructose 6 phosphate Pfam PF10432 Pfam clan ... 1pgi TCDB OPM family OPM protein CAZy CDD PBB geneid 2821 Glucose 6 phosphate isomerase , alternatively known as phosphoglucose isomerase or phosphohexose isomerase , is an enzyme that catalyzes the conversion ... Entrez Gene GPI glucose phosphate isomerase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch ... encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. The protein ... isomerase expression in human lung carcinomas journal J. Pathol. volume 210 issue 4 pages 431 40 year ... factor is the neuroleukin phosphohexose isomerase polypeptide journal Cancer Res. volume 56 issue ... foward enzyme Phosphoglucose isomerase reverse enzyme Phosphoglucose isomerase substrate small ... reaction R00771 As a glucose isomerase Enzymatic Reaction foward enzyme Phosphoglucose isomerase reverse enzyme Phosphoglucose isomerase substrate small D small Glucose product small D small Fructose ... Alpha d fructose.svg Other functions There is evidence that phosphoglucose isomerase acts as a molecular ... of several different cell types. Pathology A deficiency of phosphoglucose isomerase is responsible ... 6 phosphate isomerase In some archaea and bacteria glucose 6 phosphate isomerase PGI activity occurs via a bifunctional enzyme that also exhibits phosphomannose isomerase PMI activity. Though not closely ... title A novel phosphoglucose isomerase PGI phosphomannose isomerase from the crenarchaeon Pyrobaculum ... M title Glucose 6 phosphate isomerase deficiency. journal Baillieres Best Pract. Res. Clin. Haematol ... P, Morgan MJ title Characterization of the 5 end of the gene for human glucose phosphate isomerase ... more details
enzyme Name mannose isomerase EC number 5.3.1.7 CAS number 9031 25 8 IUBMB EC number 5 3 1 7 GO code 0050089 image width caption In enzymology , a mannose isomerase EC number 5.3.1.7 is an enzyme that catalysis catalyzes the chemical reaction D mannose math rightleftharpoons math D fructose Hence, this enzyme has one substrate biochemistry substrate , D mannose , and one product chemistry product , D fructose . This enzyme belongs to the family of isomerase s, specifically those intramolecular oxidoreductase s interconverting aldose s and ketose s. The systematic name of this enzyme class is D mannose aldose ketose isomerase . Other names in common use include D mannose isomerase , and D mannose ketol isomerase . This enzyme participates in fructose and mannose metabolism . References reflist 1 cite journal author Palleroni NJ and Doudoroff M date 1956 title Mannose isomerase of Pseudomonas saccharophila journal J. Biol. Chem. volume 218 pages 535&ndash 548 pmid 13278359 isomerase stub Category EC 5.3.1 Category Enzymes of unknown structure ... more details
enzyme Name retinal isomerase EC number 5.2.1.3 CAS number 9023 76 1 IUBMB EC number 5 2 1 3 GO code 0004744 image width caption In enzymology , a retinal isomerase EC number 5.2.1.3 is an enzyme that catalysis catalyzes the chemical reaction all trans retinal math rightleftharpoons math 11 cis retinal Hence, this enzyme has one substrate biochemistry substrate , all trans retinal , and one product chemistry product , 11 cis retinal . This enzyme belongs to the family of isomerase s, specifically Cis trans isomerism cis trans isomerases . The systematic name of this enzyme class is all trans retinal 11 cis trans isomerase . Other names in common use include retinene isomerase , and retinoid isomerase . This enzyme participates in retinol metabolism . References reflist 1 cite journal author HUBBARD R date 1956 title Retinene isomerase journal J. Gen. Physiol. volume 39 pages 935&ndash 62 pmid 13346046 doi 10.1085 jgp.39.6.935 issue 6 pmc 2147571 cite journal author Shichi H, Somers RL date 1974 title Possible involvement of retinylidene phospholipid in photoisomerization of all trans retinal to 11 cis retinal journal J. Biol. Chem. volume 249 pages 6570&ndash 7 pmid 4472816 issue 20 isomerase stub Category EC 5.2.1 Category Enzymes of unknown structure ... more details
enzyme Name ribose isomerase EC number 5.3.1.20 CAS number 57534 76 6 IUBMB EC number 5 3 1 20 GO code 0050261 image width caption In enzymology , a ribose isomerase EC number 5.3.1.20 is an enzyme that catalysis catalyzes the chemical reaction D ribose math rightleftharpoons math D ribulose Hence, this enzyme has one substrate biochemistry substrate , D ribose , and one product chemistry product , D ribulose . This enzyme belongs to the family of isomerase s, specifically those intramolecular oxidoreductase s interconverting aldose s and ketose s. The systematic name of this enzyme class is D ribose aldose ketose isomerase . Other names in common use include D ribose isomerase , and D ribose ketol isomerase . References reflist 1 cite journal author Izumori K, Rees AW, Elbein AD date 1975 title Purification, crystallization, and properties of D ribose isomerase from Mycobacterium smegmatis journal J. Biol. Chem. volume 250 pages 8085&ndash 7 pmid 240851 issue 20 isomerase stub Category EC 5.3.1 Category Enzymes of unknown structure ... more details
enzyme Name glucuronate isomerase EC number 5.3.1.12 CAS number 9023 87 4 IUBMB EC number 5 3 1 12 GO code 0008880 image width caption In enzymology , a glucuronate isomerase EC number 5.3.1.12 is an enzyme that catalysis catalyzes the chemical reaction D glucuronate math rightleftharpoons math D fructuronate Hence, this enzyme has one substrate biochemistry substrate , D glucuronate , and one product chemistry product , D fructuronate . This enzyme belongs to the family of isomerase s, specifically those intramolecular oxidoreductase s interconverting aldose s and ketose s. The systematic name of this enzyme class is D glucuronate aldose ketose isomerase . Other names in common use include uronic isomerase , uronate isomerase , D glucuronate isomerase , uronic acid isomerase , and D glucuronate ketol isomerase . This enzyme participates in pentose and glucuronate interconversions . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1J5S and PDB link 2Q01 . References reflist 1 cite journal author Ashwell G, Wahba AJ and Hickman J year 1960 title Uronic acid metabolism in bacteria. I. Purification and properties of uronic acid isomerase in Escherichia coli journal J. Biol. Chem. volume 235 pages 1559&ndash 1565 pmid 13794771 cite journal author KILGORE WW, STARR MP year 1959 title Catabolism of galacturonic and glucuronic acids by Erwinia carotovora journal J. Biol. Chem. volume 234 pages 2227&ndash 35 pmid 14409051 Category EC 5.3.1 Category Enzymes of known structure isomerase stub ... more details
enzyme Name arabinose 5 phosphate isomerase EC number 5.3.1.13 CAS number 9023 86 3 IUBMB EC number 5 3 1 13 GO code 0019146 image width caption In enzymology , an arabinose 5 phosphate isomerase EC number 5.3.1.13 is an enzyme that catalysis catalyzes the chemical reaction D arabinose 5 phosphate math rightleftharpoons math D ribulose 5 phosphate Hence, this enzyme has one substrate biochemistry substrate , D arabinose 5 phosphate , and one product chemistry product , D ribulose 5 phosphate . This enzyme belongs to the family of isomerase s, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is D arabinose 5 phosphate aldose ketose isomerase . Other names in common use include arabinose phosphate isomerase , phosphoarabinoisomerase , and D arabinose 5 phosphate ketol isomerase . References reflist 1 cite journal author Volk WA date 1960 title Purification and properties of phosphoarabinoisomerase from Propionibacterium pentosaceum journal J. Biol. Chem. volume 235 pages 1550&ndash 1553 isomerase stub Category EC 5.3.1 Category Enzymes of unknown structure ... more details
enzyme Name linoleate isomerase EC number 5.2.1.5 CAS number 37318 41 5 IUBMB EC number 5 2 1 5 GO code 0050058 image width caption In enzymology , a linoleate isomerase EC number 5.2.1.5 is an enzyme that catalysis catalyzes the chemical reaction 9 cis,12 cis octadecadienoate math rightleftharpoons math 9 cis,11 trans octadecadienoate Hence, this enzyme has one substrate biochemistry substrate , 9 cis,12 cis octadecadienoate , and one product chemistry product , 9 cis,11 trans octadecadienoate . This enzyme belongs to the family of isomerase s, specifically Cis trans isomerism cis trans isomerases . The systematic name of this enzyme class is linoleate Delta12 cis Delta11 trans isomerase . This enzyme is also called linoleic acid isomerase . This enzyme participates in linoleic acid metabolism . References reflist 1 cite journal author Kepler CR, Tove SB date 1967 title Biohydrogenation of unsaturated fatty acids. 3. Purification and properties of a linoleate delta 12 cis, delta 11 trans isomerase from Butyrivibrio fibrisolvens journal J. Biol. Chem. volume 242 pages 5686&ndash 92 pmid 5633396 issue 24 isomerase stub Category EC 5.2.1 Category Enzymes of unknown structure ... more details
enzyme Name hydroxypyruvate isomerase EC number 5.3.1.22 CAS number 74812 48 9 IUBMB EC number 5 3 1 22 GO code 0008903 image width caption In enzymology , a hydroxypyruvate isomerase EC number 5.3.1.22 is an enzyme that catalysis catalyzes the chemical reaction hydroxypyruvate math rightleftharpoons math 2 hydroxy 3 oxopropanoate Hence, this enzyme has one substrate biochemistry substrate , hydroxypyruvate , and one product chemistry product , 2 hydroxy 3 oxopropanoate . This enzyme belongs to the family of isomerase s, specifically those intramolecular oxidoreductase s interconverting aldose s and ketose s. The systematic name of this enzyme class is hydroxypyruvate aldose ketose isomerase . This enzyme participates in glyoxylate and dicarboxylate metabolism . References reflist 1 cite journal author de Windt FE, van der Drift C date 1980 title Purification and some properties of hydroxypyruvate isomerase of Bacillus fastidiosus journal Biochim. Biophys. Acta. volume 613 pages 556&ndash 62 pmid 7448201 issue 2 isomerase stub Category EC 5.3.1 Category Enzymes of unknown structure ... more details
enzyme Name thiocyanate isomerase EC number 5.99.1.1 CAS number 9023 71 6 IUBMB EC number 5 99 1 1 GO code 0050335 image width caption In enzymology , a thiocyanate isomerase EC number 5.99.1.1 is an enzyme that catalysis catalyzes the chemical reaction benzyl isothiocyanate math rightleftharpoons math benzyl thiocyanate Hence, this enzyme has one substrate biochemistry substrate , benzyl isothiocyanate , and one product chemistry product , benzyl thiocyanate . This enzyme belongs to the family of isomerase s, specifically those other isomerases sole sub subclass for isomerases that do not belong in the other subclasses. The systematic name of this enzyme class is benzyl thiocyanate isomerase . This enzyme is also called isothiocyanate isomerase . References reflist 1 cite journal author Virtanen AI date 1962 title On enzymic and chemical reactions in crushed plants journal Arch. Biochem. Biophys. Suppl. volume 1 pages 200&ndash 208 isomerase stub Category EC 5.99.1 Category Enzymes of unknown structure ... more details
enzyme Name S methyl 5 thioribose 1 phosphate isomerase EC number 5.3.1.23 CAS number 91608 95 6 IUBMB EC number 5 3 1 23 GO code 0046523 image width caption In enzymology , a S methyl 5 thioribose 1 phosphate isomerase EC number 5.3.1.23 is an enzyme that catalysis catalyzes the chemical reaction S methyl 5 thio alpha D ribose 1 phosphate math rightleftharpoons math S methyl 5 thio D ribulose 1 phosphate Hence, this enzyme has one substrate biochemistry substrate , S methyl 5 thio alpha D ribose 1 phosphate , and one product chemistry product , S methyl 5 thio D ribulose 1 phosphate . This enzyme belongs to the family of isomerase s, specifically those intramolecular oxidoreductase s interconverting aldose s and ketose s. The systematic name of this enzyme class is S methyl 5 thio alpha D ribose 1 phosphate aldose ketose isomerase . Other names in common use include methylthioribose 1 phosphate isomerase , 1 PMTR isomerase , 5 methylthio 5 deoxy D ribose 1 phosphate ketol isomerase , S methyl 5 thio 5 deoxy D ribose 1 phosphate ketol isomerase , S methyl 5 thio 5 deoxy D ribose 1 phosphate , aldose ketose isomerase , 1 phospho 5 S methylthioribose isomerase , and S methyl 5 thio D ribose 1 phosphate aldose ketose isomerase . This enzyme participates in methionine metabolism . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1T9K and PDB link 1W2W . References reflist 1 cite journal author RH date 1984 title Characterization of a defect in the pathway for converting 5 deoxy 5 methylthioadenosine to methionine in a subline of a cultured heterogeneous human colon carcinoma journal J. Biol. Chem. volume 259 pages 6715&ndash 9 pmid 6725268 last2 Savarese first2 TM last3 Dexter first3 DL last4 Parks Jr first4 RE last5 Trackman first5 PC last6 Abeles first6 RH ... issue 20 isomerase stub Category EC 5.3.1 Category Enzymes of known structure ... more details
enzyme Name arabinose isomerase EC number 5.3.1.3 CAS number 9023 81 8 IUBMB EC number 5 3 1 3 GO code 0008790 image width caption In enzymology , an arabinose isomerase EC number 5.3.1.3 is an enzyme that catalysis catalyzes the chemical reaction D arabinose math rightleftharpoons math D ribulose Hence, this enzyme has one substrate biochemistry substrate , D arabinose , and one product chemistry product , D ribulose . This enzyme belongs to the family of isomerase s, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is D arabinose aldose ketose isomerase . Other names in common use include D arabinose L fucose isomerase , D arabinose isomerase , L fucose isomerase , and D arabinose ketol isomerase . 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 1FUI . References reflist 1 cite journal author Cohen SS date 1953 title Studies on D ribulose and its enzymatic conversion to D arabinose journal J. Biol. Chem. volume 201 issue 1 pages 71&ndash 84 pmid 13044776 cite journal author Green M and Cohen SS date 1956 title Enzymatic conversion of L fucose to L fuculose journal J. Biol. Chem. volume 219 issue 2 pages 557&ndash 568 pmid 13319278 isomerase stub Category EC 5.3.1 Category Enzymes of known structure ... more details
enzyme Name maleylacetoacetate isomerase EC number 5.2.1.2 CAS number 9023 75 0 IUBMB EC number 5 2 1 2 GO code 0016034 image width caption In enzymology , a maleylacetoacetate isomerase EC number 5.2.1.2 is an enzyme that catalysis catalyzes the chemical reaction 4 maleylacetoacetate math rightleftharpoons math 4 fumarylacetoacetate Hence, this enzyme has one substrate biochemistry substrate , 4 Maleylacetoacetate 4 maleylacetoacetate , and one product chemistry product , 4 fumarylacetoacetate . This enzyme belongs to the family of isomerase s, specifically Cis trans isomerism cis trans isomerases . The systematic name of this enzyme class is 4 maleylacetoacetate cis trans isomerase . Other names in common use include maleylacetoacetic isomerase , maleylacetone isomerase , and maleylacetone cis trans isomerase . This enzyme participates in tyrosine metabolism and styrene degradation . 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 1FW1 , PDB link 2CZ2 , and PDB link 2CZ3 . References reflist 1 cite journal author EDWARDS SW, KNOX WE date 1956 title Homogentisate metabolism the isomerization of maleylacetoacetate by an enzyme which requires glutathione journal J. Biol. Chem. volume 220 pages 79&ndash 91 pmid 13319328 issue 1 cite journal author Lack L date 1961 title Enzymic cis trans isomerization of maleylpyruvic acid journal J. Biol. Chem. volume 236 pages 2835&ndash 2840 pmid 14461395 cite journal author Seltzer S date 1973 title Purification and properties of maleylacetone cis trans isomerase from vibrio 01 journal J. Biol. Chem. volume 248 pages 215&ndash 22 pmid 4692831 issue 1 isomerase stub Category EC 5.2.1 Category Enzymes of known structure ... more details
enzyme Name chalcone isomerase EC number 5.5.1.6 CAS number 9073 57 8 IUBMB EC number 5 5 1 6 GO code 0045430 image width caption Infobox protein family Symbol Chalcone Name Chalcone isomerase image PDB 1jep EBI.jpg width caption chalcone isomerase complexed with 4 hydroxyflavanone Pfam PF02431 Pfam clan InterPro IPR003466 SMART PROSITE MEROPS SCOP 1eyp TCDB OPM family OPM protein CAZy CDD In enzymology , a chalcone isomerase EC number 5.5.1.6 is an enzyme that catalysis catalyzes the chemical reaction a chalcone math rightleftharpoons math a flavanone Hence, this enzyme has one substrate biochemistry substrate , a chalconoid chalcone , and one product chemistry product , a flavanone . This enzyme belongs to the family of isomerase s, specifically the class of intramolecular lyases. The systematic name of this enzyme class is flavanone lyase decyclizing . This enzyme is also called chalcone flavanone isomerase . This enzyme participates in flavonoid biosynthesis . The Petunia hybrida Petunia genome contains two genes coding for very similar enzymes, ChiA and ChiB, but only the first seems to encode a functional chalcone isomerase. Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EYP , PDB link 1EYQ , PDB link 1FM7 , PDB link 1FM8 , PDB link 1JEP , PDB link 1JX0 , and PDB link 1JX1 . Chalcone isomerase has a core 2 layer alpha beta secondary structure structure consisting of beta 3 alpha 2 beta alpha 2 beta 3 . ref name pmid10966651 cite journal author Jez JM, Bowman ME, Dixon RA, Noel JP title Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase journal Nat. Struct. Biol. volume 7 issue 9 pages 786 91 year 2000 month September ... author Moustafa E and Wong E year 1967 title Purification and properties of chalcone flavanone isomerase ... EC 5.5.1 Category Enzymes of known structure isomerase stub ... more details
enzyme Name furylfuramide isomerase EC number 5.2.1.6 CAS number 72561 07 0 IUBMB EC number 5 2 1 6 GO code 0047907 image width caption In enzymology , a furylfuramide isomerase EC number 5.2.1.6 is an enzyme that catalysis catalyzes the chemical reaction E 2 2 furyl 3 5 nitro 2 furyl acrylamide math rightleftharpoons math Z 2 2 furyl 3 5 nitro 2 furyl acrylamide Hence, this enzyme has one substrate biochemistry substrate , E 2 2 furyl 3 5 nitro 2 furyl acrylamide , and one product chemistry product , Z 2 2 furyl 3 5 nitro 2 furyl acrylamide . This enzyme belongs to the family of isomerase s, specifically Cis trans isomerism cis trans isomerases . The systematic name of this enzyme class is 2 2 furyl 3 5 nitro 2 furyl acrylamide cis trans isomerase . It has 2 cofactor biochemistry cofactors NAD , and NADH . References reflist 1 cite journal author Tomoeda M, Kitamura R year 1977 title A cis trans isomerising activity of Escherichia coli. Isomerization from 2 2 furyl 3 cis 5 nitro 2 furyl acrylamide furylfuramide to its trans isomer journal Biochim. Biophys. Acta. volume 480 pages 315&ndash 25 pmid 12827 issue 1 Category EC 5.2.1 Category NADH dependent enzymes Category Enzymes of unknown structure isomerase stub ... more details
enzyme Name maleylpyruvate isomerase EC number 5.2.1.4 CAS number 9023 77 2 IUBMB EC number 5 2 1 4 GO code 0050077 image width caption In enzymology , a maleylpyruvate isomerase EC number 5.2.1.4 is an enzyme that catalysis catalyzes the chemical reaction 3 maleylpyruvate math rightleftharpoons math 3 fumarylpyruvate Hence, this enzyme has one substrate biochemistry substrate , 3 maleylpyruvate , and one product chemistry product , 3 fumarylpyruvate . This enzyme belongs to the family of isomerase s, specifically Cis trans isomerism cis trans isomerases . The systematic name of this enzyme class is 3 maleylpyruvate cis trans isomerase . This enzyme participates in tyrosine metabolism . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2NSF and PDB link 2NSG . References reflist 1 cite journal author Lack L date 1961 title Enzymic cis trans isomerization of maleylpyruvic acid journal J. Biol. Chem. volume 236 pages 2835&ndash 2840 pmid 14461395 isomerase stub Category EC 5.2.1 Category Enzymes of known structure ... more details
enzyme Name retinol isomerase EC number 5.2.1.7 CAS number 109740 80 9 IUBMB EC number 5 2 1 7 GO code 0050251 image width caption In enzymology , a retinol isomerase EC number 5.2.1.7 is an enzyme that catalysis catalyzes the chemical reaction all trans retinol math rightleftharpoons math 11 cis retinol Hence, this enzyme has one substrate biochemistry substrate , all trans retinol , and one product chemistry product , 11 cis retinol . This enzyme belongs to the family of isomerase s, specifically Cis trans isomerism cis trans isomerases . The systematic name of this enzyme class is all trans retinol 11 cis trans isomerase . This enzyme is also called all trans retinol isomerase . This enzyme participates in retinol metabolism . References reflist 1 cite journal author Bernstein PS, Law WC, Rando RR date 1987 title Isomerization of all trans retinoids to 11 cis retinoids in vitro journal Proc. Natl. Acad. Sci. U. S. A. volume 84 pages 1849&ndash 53 pmid 3494246 doi 10.1073 pnas.84.7.1849 issue 7 pmc 304538 cite journal author Bridges CD, Alvarez RA date 1987 title The visual cycle operates via an isomerase acting on all trans retinol in the pigment epithelium journal Science. volume 236 pages 1678&ndash 80 pmid 3603006 doi 10.1126 science.3603006 issue 4809 isomerase stub Category EC 5.2.1 Category Enzymes of unknown structure ... more details
enzyme Name maleate isomerase EC number 5.2.1.1 CAS number 9023 74 9 IUBMB EC number 5 2 1 1 GO code 0050076 image width caption In enzymology , a maleate isomerase EC number 5.2.1.1 is an enzyme that catalysis catalyzes the chemical reaction maleate math rightleftharpoons math fumarate Hence, this enzyme has one substrate biochemistry substrate , maleate , and one product chemistry product , fumarate . This enzyme belongs to the family of isomerase s, specifically Cis trans isomerism cis trans isomerases . The systematic name of this enzyme class is maleate cis trans isomerase . This enzyme participates in butanoate metabolism and nicotinate and nicotinamide metabolism . References reflist 1 cite journal author Behrmann EJ, Stanier RY date 1957 title The bacterial oxidation of nicotinic acid journal J. Biol. Chem. volume 228 pages 923&ndash 45 pmid 13475371 issue 2 cite journal author Scher W, Jakoby WB date 1969 title Maleate isomerase journal J. Biol. Chem. volume 244 pages 1878&ndash 82 pmid 5780844 issue 7 cite journal author Hatakeyama K, Asai Y, Uchida Y, Kobayashi M, Terasawa M, Yukawa H date 1997 title Gene cloning and characterization of maleate cis trans isomerase from Alcaligenes faecalis journal Biochem. Biophys. Res. Commun. volume 239 pages 74&ndash 9 pmid 9345272 issue 1 doi 10.1006 bbrc.1997.7430 cite journal author Hatakeyama K, Goto M, Uchida Y, Kobayashi M, Terasawa M, Yukawa H date 2000 title Molecular analysis of maleate cis trans isomerase from thermophilic bacteria journal Biochem. Biophys. Res. Commun. volume 64 pages 569&ndash 76 pmid 10803955 issue 3 doi 10.1271 bbb.64.569 cite journal author Fisch F, Fleites CM, Delenne M, Baudendistel N, Hauer B, Turkenburg JP, Hart S, Bruce NC, Grogan G date 2010 title A covalent succinylcysteine like intermediate in the enzyme catalyzed transformation of maleate to fumarate by maleate isomerase journal J. Am. Chem. Soc. volume 132 pages 11455&ndash 7 pmid 20677745 issue 33 doi 10.1021 ja1053576 isomerase ... more details
protein name triosephosphate isomerase 1 caption The structure of human TPI PDB 1WYI image width HGNCid ... 12 Arm p Band 13 LocusSupplementaryData Triose phosphate isomerase TPI or TIM , is an enzyme ... Ribbon pastel whitebkg.jpg thumb 300px Side view of triose P isomerase monomer, active site at top center Enzymatic Reaction foward enzyme triose phosphate isomerase reverse enzyme triose phosphate isomerase substrate Dihydroxyacetone phosphate product small D small glyceraldehyde 3 phosphate reaction ..., severe neurological disorder called Triose Phosphate Isomerase deficiency triose phosphate isomerase deficiency . Triose phosphate isomerase deficiency is characterized by chronic hemolytic ... Ol h, J. title Triosephosphate isomerase deficiency facts and doubts journal IUBMB Life volume ... pmid 17424909 unused data DUPLICATE DATA coauthors Ov di, J. ref Triose phosphate isomerase is a highly ... Free Energy Profile for the Reaction Catalyzed by Triosephosphate Isomerase journal Biochemistry ... diffusion in the active site of triosephosphate isomerase journal Biochemistry volume 29 issue ... Isomerase DeltaG.svg Free energy changes The structure of TPI facilitates the conversion between ... mechanism of triose phosphate isomerase. journal Phil. Trans. R. Soc. volume 293 issue 1063 pages ... coauthors Davenport, R.C. title Triose Phosphate Isomerase Removal of a Putatively Electrophilic ... E.A. authorlink coauthors Chang, L.C. title Electrophilic Catalysis in Triosephosphate Isomerase ... Phosphate Isomerase Mechanism TPI is diffusion limited. In terms of thermodynamics, DHAP formation ... Cole, R.N. title Proton Transfer in the Mechanism of Triosephosphate Isomerase. journal Biochemistry ... phosphate isomerase from Trypanosama brucei brucei journal European Journal of Biochemistry volume ... of the Complex between Triosephosphate Isomerase and 2 Phosphoglycolate at 2.5 Resolution Implications ... 300px Side view of triose phosphate isomerase dimer. Structure Triose phosphate isomerase is a protein ... more details
Merge from FKBP date November 2010 enzyme Name Peptidylprolyl isomerase EC number 5.2.1.8 CAS number 95076 93 0 IUBMB EC number 5 2 1 8 GO code 0003755 image width caption Pfam box Symbol PPIase PpiC image PDB 1nmw EBI.jpg Name Peptidyl prolyl cis trans isomerase, PpiC type Pfam PF00639 InterPro IPR000297 PROSITE PDOC00840 PDB PDB 1eq3 PDB 1f8a PDB 1fjd PDB 1j6y PDB 1jns PDB 1jnt PDB 1m5y PDB 1nmv PDB 1nmw Prolyl isomerase also known as peptidylprolyl isomerase or PPIase is an enzyme EC number 5.2.1.8 found in both prokaryote s and eukaryote s that interconverts the cis and trans Cis trans isomerism isomer s of peptide bond s with the amino acid proline . ref name PUB00000320 cite journal author Fischer G, Schmid FX title The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell journal Biochemistry volume 29 issue 9 pages 2205 2212 year 1990 pmid 2186809 doi 10.1021 bi00461a001 ref Proline has an unusually conformationally restrained peptide bond due to its cyclic structure with its side chain bonded to its secondary amine nitrogen. Most amino acid s have a strong energetic preference for the trans peptide bond conformation due to steric hindrance, but proline s unusual structure stabilizes the cis form so that both isomers are populated under biologically relevant conditions. Proteins with prolyl isomerase ... prolyl isomerase structural domain domains . Protein folding Proline is unique among the natural amino ... , and some interleukin s. Prolyl isomerase folding can be autocatalytic and therefore the speed of folding ... of a prolyl isomerase. Acceleration of the in vitro folding rate in mutation mutant protein ... of prolines in certain sequence contexts. Assays for prolyl isomerase activity Prolyl isomerase ... isomerase will accelerate this latter reaction phase if it has true prolyl isomerase activity. References ... isomerases DEFAULTSORT Prolyl Isomerase Category EC 5.2.1 de Peptidyl Prolyl cis trans Isomerasen ja ... more details
enzyme Name phosphoribosylanthranilate isomerase EC number 5.3.1.24 CAS number 37259 82 8 IUBMB EC number 5 3 1 24 GO code 0004640 image width caption Infobox protein family Symbol PRAI Name PRAI image PDB 1dl3 EBI.jpg width caption crystal structure of mutually generated monomers of dimeric phosphoribosylantranilate isomerase from thermotoga maritima Pfam PF00697 Pfam clan CL0036 InterPro IPR001240 SMART PROSITE MEROPS SCOP 1pii TCDB OPM family OPM protein CAZy CDD In enzymology , a phosphoribosylanthranilate isomerase EC number 5.3.1.24 is an enzyme that catalysis catalyzes the third step of tryptophan biosynthesis . ref cite journal author Creighton TE and Yanofsky C date 1970 title Chorismate to tryptophan Escherichia coli Anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase journal Methods Enzymol. volume 17A pages 365&ndash 380 ref N 5 phospho beta D ribosyl anthranilate math rightleftharpoons math 1 2 carboxyphenylamino 1 deoxy D ribulose 5 phosphate Hence, this enzyme has one substrate biochemistry substrate , N 5 phospho beta D ribosyl anthranilate , and one product chemistry product , 1 2 carboxyphenylamino 1 deoxy D ribulose 5 phosphate . This enzyme belongs to the family of isomerase s, specifically those intramolecular oxidoreductase ... beta D ribosyl anthranilate aldose ketose isomerase . Other names in common use include PRA isomerase , PRAI , IGPS PRAI indole 3 glycerol phosphate , synthetase N 5 phosphoribosylanthranilate isomerase complex , and N 5 phospho beta D ribosyl anthranilate ketol isomerase . This enzyme participates ... isomerase PRAI is monomeric and labile in most mesophilic microorganisms, but protein dimer ... generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima journal ... at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima ... InterPro content IPR001240 isomerase stub Category EC 5.3.1 Category Enzymes of known structure Category ... more details
enzyme Name galactose 6 phosphate isomerase EC number 5.3.1.26 CAS number 39433 98 2 IUBMB EC number 5 3 1 26 GO code 0050044 image width caption In enzymology , a galactose 6 phosphate isomerase EC number 5.3.1.26 is an enzyme that catalysis catalyzes the chemical reaction D galactose 6 phosphate math rightleftharpoons math D tagatose 6 phosphate Hence, this enzyme has one substrate biochemistry substrate , D galactose 6 phosphate , and one product chemistry product , D tagatose 6 phosphate . This enzyme belongs to the family of isomerase s, specifically those intramolecular oxidoreductase s interconverting aldose s and ketose s. The systematic name of this enzyme class is D galactose 6 phosphate aldose ketose isomerase . This enzyme participates in galactose metabolism . References reflist 1 cite journal author de Vos WM, Boerrigter I, van Rooyen RJ, Reiche B, Hengstenberg W date 1990 title Characterization of the lactose specific enzymes of the phosphotransferase system in Lactococcus lactis journal J. Biol. Chem. volume 265 pages 22554&ndash 60 pmid 2125052 issue 36 cite journal author van Rooijen RJ, van Schalkwijk S, de Vos WM date 1991 title Molecular cloning, characterization, and nucleotide sequence of the tagatose 6 phosphate pathway gene cluster of the lactose operon of Lactococcus lactis journal J. Biol. Chem. volume 266 pages 7176&ndash 81 pmid 1901863 issue 11 isomerase stub Category EC 5.3.1 Category Enzymes of unknown structure ... more details
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