infobox enzyme Name triosephosphateisomerase EC number 5.3.1.1 CAS number 9023 78 3 IUBMB EC number ... for the Reaction Catalyzed by TriosephosphateIsomerase journal Biochemistry volume 15 issue 25 pages ... site of triosephosphateisomerase journal Biochemistry volume 29 issue 18 pages 4312 4317 publisher ..., and are displayed in the figure. ref name albery Image TriosephosphateIsomerase DeltaG.svg ... Chang, L.C. title Electrophilic Catalysis in TriosephosphateIsomerase the Role of Histidine 95 ... Transfer in the Mechanism of TriosephosphateIsomerase. journal Biochemistry volume 37 issue 47 pages ... TriosephosphateIsomerase and 2 Phosphoglycolate at 2.5 Resolution Implications for Catalysis journal ... phosphate isomerase dimer. Structure Infobox protein family Symbol TIM Name Triosephosphateisomerase ... authorlink coauthors Chang, L.C. title TriosephosphateIsomerase Requires a Positively Charged Active ... TPI1 http www.proteopedia.org wiki index.php TriosephosphateIsomeraseTriosephosphateisomerase in interactive 3D at Proteopedia http www.expasy.org prosite PDOC00155 Triosephosphateisomerase TIM ... view of triose P isomerase monomer, active site at top center Triose phosphate isomerase TPI or TIM ... foward enzyme triose phosphate isomerase reverse enzyme triose phosphate isomerase substrate Dihydroxyacetone ... disorder called Triose Phosphate Isomerase deficiency triose phosphate isomerase deficiency . Triose phosphate isomerase deficiency is characterized by chronic hemolytic anemia . While there are various ... 104 to aspartic acid. ref cite journal last Orosz first F. authorlink coauthors Ol h, J. title Triosephosphateisomerase deficiency facts and doubts journal IUBMB Life volume 58 issue 12 pages 703 ... data DUPLICATE DATA coauthors Ov di, J. ref Triose phosphate isomerase is a highly efficient enzyme ... isomerase. journal Phil. Trans. R. Soc. volume 293 issue 1063 pages 159 171 publisher year 1981 ..., R.C. title Triose Phosphate Isomerase Removal of a Putatively Electrophilic Histidine Residue Results ... more details
Infobox disease Name Triosephosphateisomerase deficiency Image Caption DiseasesDB 30116 ICD10 ICD10 D 55 2 d 55 ICD9 ICD9 282.3 ICDO OMIM 190450 MedlinePlus eMedicineSubj eMedicineTopic MeshID Triosephosphateisomerase deficiency is a rare autosome autosomal dominance genetics recessive ref name Ralser et al 2006 inborn errors of metabolism metabolic disorder which was initially described in 1965. ref name Schneider et al 1965 cite journal doi 10.1056 NEJM196502042720503 last Schneider first Arthur S. coauthors William N. Valentine, Hattori M, H. L. Heins Jr year 1965 title Hereditary Hemolytic Anemia with TriosephosphateIsomerase Deficiency journal New England Journal of Medicine volume 272 issue 5 pages 229 235 pmid 14242501 ref It is a unique glycolysis glycolytic enzymopathy that is characterized by chronic haemolytic anaemia , cardiomyopathy , susceptibility to infections, severe neurological dysfunction, and, in most cases, death in early childhood. ref name Schneider 2000 cite journal last Schneider first Arthur S. year 2000 month Mar title Triosephosphateisomerase deficiency historical perspectives and molecular aspects volume 13 issue 1 pages 119 140 pmid 10916682 doi 10.1053 beha.2000.0061 url http www.sciencedirect.com science? ob ArticleURL& udi B6WBG 45FKMG0 1M& coverDate 03 2F31 2F2000& alid 513209010& rdoc 1& fmt & orig search& qd 1& cdi 6710& sort d&view c& acct ... thumb right Triosephosphateisomerase deficiency has an autosomal recessive pattern of inheritance ... and encodes the ubiquitous housekeeping enzyme triosephosphateisomerase TPI , have been discovered ... The 1591C mutation in triosephosphateisomerase TPI deficiency. Tightly linked polymorphisms and a common ... date December 20, 2006 editor1 last Janbon editor1 first Guilhem title Triose Phosphate Isomerase Deficiency ... Rare diseases genetic disorder stub de Triosephosphat Isomerase Defizienz pl Niedob r izomerazy fosfotriozowej pt Defici ncia de triose fosfato isomerase ... 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
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 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 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 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 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 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 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 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 xylose isomerase EC number 5.3.1.5 CAS number 9023 82 9 IUBMB EC number 5 3 1 5 GO code 0009045 image 2glk.png width caption D Xylose isomerase tetramer from Streptomyces rubiginosus Protein Data Bank PDB PDBe 2glk ref cite pmid 16707576 ref . One monomer is coloured by secondray structure to highlight the TIM barrel architecture. In enzymology , a xylose isomerase 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 xylose isomerase , 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 Xylose isomerase enzymes exhibit a TIM barrel fold with the active site in the centre of the barrel and a tetrameric quaternary structure ref http www.ebi.ac.uk pdbe srv PDBeXplore enzyme ?ec 5.3.1.5&tab assemblies ref . PDB structures are available in the links in the infobox to the right. References reflist 1 cite journal author HOCHSTER RM, WATSON RW date 1954 title Enzymatic isomerization of D xylose to D xylulose journal Arch. Biochem. Biophys. volume 48 pages 120&ndash 9 pmid 13125579 doi 10.1016 0003 9861 54 90313 6 issue 1 cite journal author Slein MW date 1955 title Xylose isomerase from Pasteurella pestis, strain A 1122 journal J. Am. Chem. Soc. volume 77 pages ..., crystallization and properties of the D xylose isomerase from Lactobacillus brevis journal Biochim. Biophys. Acta. volume 151 pages 670&ndash 80 pmid 5646045 issue 3 isomerase stub Category ... 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 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
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
Distinguish D xylose isomerase 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 ... glucose phosphate isomerase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch ... multifunctional phosphoglucose isomerase proteins involved in energy pathways. The protein encoded by this gene ... and pathological significance of autocrine motility factor glucose 6 phosphate isomerase expression ... phosphohexose isomerase polypeptide journal Cancer Res. volume 56 issue 13 pages 2960 ... Phosphoglucose isomerase reverse enzyme Phosphoglucose isomerase substrate small D small Glucose ... Isomerization of glucose Enzymatic Reaction foward enzyme Phosphoglucose isomerase reverse enzyme Phosphoglucose isomerase substrate small D small Glucose product small D small Fructose reaction direction ... Mechanism The mechanism of glucose 6 phosphate isomerase involves the formation of an enediol ... isomerase and phosphomannose isomerase date 12 year 1956 month Sep url www.jbc.org content 225 1 419.full.pdf ref 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 ... 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 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 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
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
PBB geneid 5478 Peptidylprolyl isomerase A also known as cyclophilin A or rotamase A is an enzyme that in humans is encoded by the PPIA gene . ref name entrez ref name pmid2197089 cite journal author Haendler B, Hofer E title Characterization of the human cyclophilin gene and of related processed pseudogenes journal Eur. J. Biochem. volume 190 issue 3 pages 477 82 year 1990 month July pmid 2197089 doi 10.1111 j.1432 1033.1990.tb15598.x ref ref name pmid1989998 cite journal author Holzman TF, Egan DA, Edalji R, Simmer RL, Helfrich R, Taylor A, Burres NS title Preliminary characterization of a cloned neutral isoelectric form of the human peptidyl prolyl isomerase cyclophilin journal J. Biol. Chem. volume 266 issue 4 pages 2474 9 year 1991 month February pmid 1989998 doi ref Function This gene encodes a member of the peptidyl prolyl cis trans isomerase PPIase family. PPIases catalyze the cis trans isomerization of proline imidic peptide bond s in oligopeptide s and accelerates the folding of protein s. The encoded protein is a cyclosporin binding protein and may play a role in cyclosporin A mediated immunosuppression . The protein can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virion s. Multiple pseudogene s that map to different chromosome s have been reported. ref name entrez cite web title Entrez Gene PPIA peptidylprolyl isomerase A cyclophilin A url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 5478 accessdate ref Interactions Peptidylprolyl isomerase A has been shown to Protein protein interaction interact with ITK gene ITK . ref name pmid11830645 cite journal last Brazin first Kristine N authorlink coauthors Mallis Robert J, Fulton D Bruce, Andreotti Amy H year 2002 month Feb. title Regulation of the tyrosine kinase Itk by the peptidyl prolyl isomerase cyclophilin A journal PNAS Proc. Natl. Acad. Sci. U.S.A. volume 99 issue ... more details
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