EzCatDB: S00545
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DB codeS00545
CATH domainDomain 13.10.450.50 : Nuclear Transport Factor 2; ChainCatalytic domain
E.C.5.3.3.1

CATH domainRelated DB codes (homologues)
3.10.450.50 : Nuclear Transport Factor 2; ChainS00176,S00177,T00024

Enzyme Name
UniProtKBKEGG

P00947
Protein nameSteroid Delta-isomerasesteroid Delta-isomerase
hydroxysteroid isomerase
steroid isomerase
Delta5-ketosteroid isomerase
Delta5(or Delta4)-3-keto steroid isomerase
Delta5-steroid isomerase
3-oxosteroid isomerase
Delta5-3-keto steroid isomerase
Delta5-3-oxosteroid isomerase
SynonymsEC 5.3.3.1
Delta(5)-3-ketosteroid isomerase
PfamPF02136 (NTF2)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00140C21-Steroid hormone metabolism
MAP00150Androgen and estrogen metabolism

UniProtKB:Accession NumberP00947
Entry nameSDIS_COMTE
ActivityA 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)- steroid.
SubunitHomodimer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC01034C00619I00017
Compound3-Oxo-delta5-steroid3-Oxo-delta4-steroid3-Hydroxy-androsta-3,5-dien
Typecarbohydrate,steroidcarbohydrate,steroid
ChEBI
47909

PubChem439372
439274

           
1buqAUnboundAnalogue:NTHUnbound
1buqBUnboundAnalogue:NTHUnbound
1iskAUnboundUnboundUnbound
1iskBUnboundUnboundUnbound
1ocvAUnboundUnboundUnbound
1ocvBUnboundUnboundUnbound
1ocvCUnboundUnboundUnbound
1ocvDUnboundUnboundUnbound
1ogzAUnboundUnboundIntermediate-analogue:EQU
1ohpAAnalogue:ESRUnboundUnbound
1ohpBAnalogue:ESRUnboundUnbound
1ohpCAnalogue:ESRUnboundUnbound
1ohpDAnalogue:ESRUnboundUnbound
1ohsAAnalogue:5SDUnboundUnbound
1ohsBAnalogue:5SDUnboundUnbound
1ohsCAnalogue:5SDUnboundUnbound
1ohsDUnboundUnboundUnbound
1qjgAUnboundUnboundIntermediate-analogue:EQU
1qjgBUnboundUnboundIntermediate-analogue:EQU
1qjgCUnboundUnboundIntermediate-analogue:EQU
1qjgDUnboundUnboundIntermediate-analogue:EQU
1qjgEUnboundUnboundIntermediate-analogue:EQU
1qjgFUnboundUnboundIntermediate-analogue:EQU
8choAUnboundUnboundUnbound

Active-site residues
resource
literature [38], [41]
pdbCatalytic residuescomment
          
1buqATYR  14;ASP  38;       ;ASP   99
mutant Y55F, Y88F
1buqBTYR 214;ASP 238;       ;ASP  299
mutant Y255F, Y288F
1iskATYR  14;ASP  38;TYR  55;ASP   99
 
1iskBTYR  14;ASP  38;TYR  55;ASP   99
 
1ocvATYR  14;ASP  38;TYR  55;ASP   99
mutant T83I, F116W
1ocvBTYR 214;ASP 238;TYR 255;ASP  299
mutant T283I, F316W
1ocvCTYR 414;ASP 438;TYR 455;ASP  499
mutant T483I, F516W
1ocvDTYR 614;ASP 638;TYR 655;ASP  699
mutant T683I, F716W
1ogzATYR  14;ASP  38;TYR  55;ASP   99
mutant P39A, T83I
1ohpATYR  14;       ;TYR  55;ASP   99
mutant D38N, T83I
1ohpBTYR 214;       ;TYR 255;ASP  299
mutant D238N, T283I
1ohpCTYR  14;       ;TYR  55;ASP   99
mutant D38N, T83I
1ohpDTYR 214;       ;TYR 255;ASP  299
mutant D238N, T283I
1ohsA       ;       ;TYR  55;ASP   99
mutant Y14F, D38N, T83I
1ohsB       ;       ;TYR 255;ASP  299
mutant Y214F, D238N, T283I
1ohsC       ;       ;TYR  55;ASP   99
mutant Y14F, D38N, T83I
1ohsD       ;       ;TYR 255;ASP  299
mutant Y214F, D238N, T283I
1qjgATYR  14;       ;TYR  55;ASP   99
mutant D38N, T83I
1qjgBTYR  14;       ;TYR  55;ASP   99
mutant D38N, T83I
1qjgCTYR  14;       ;TYR  55;ASP   99
mutant D38N, T83I
1qjgDTYR  14;       ;TYR  55;ASP   99
mutant D38N, T83I
1qjgETYR  14;       ;TYR  55;ASP   99
mutant D38N, T83I
1qjgFTYR  14;       ;TYR  55;ASP   99
mutant D38N, T83I
8choATYR  14;ASP  38;TYR  55;ASP   99
mutant T83I

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.9, p.3935-3936
[4]Fig.13, p.158-159
[5]Fig.1, p.10271, p.10276-10277
[6]Fig.1, Fig.2, Fig.6, p.7498-7500
[7]Fig.1, Fig.2, Fig.9, p.3169-3170, 3176-3178
[8]Fig.1, p.4991-4992, p.4993-4996
[9]Fig.1, Scheme 1, Fig.6, p.10859, p.10863-10865
[10]equation (1), p.694
[11]Fig.1, p.1817, p.1823
[12]Fig.1, p.2682-2683
[13]Scheme 1, Scheme 4, Scheme 8, p.12178-12182
[14]Fig.1, Fig.4, p.2678-2680
[15]Scheme 1, p.13896, p.13900-13902
[16]Scheme 1, p.14245-14246, p.14250-14252
[17]p.6569-6571
[19]Scheme 1, Scheme 4, p.15456-15458
[20]Scheme 1, Scheme 3, p.6441-6442
[21]Fig.1, p.1525-1526
[22]Fig.1, p.8220
[24]p.14033-14036
[25]Fig.1, p.14616-14617, p.14625
[26]Fig.1, p.3468-3471
[27]p.7745-7747
[28]Fig.1
[29]Scheme 1, p.417
[30]p.8329
[31]Fig.1, p.14708-14711
[32]Scheme 1, p.6763-6765
[33]Scheme 2, Scheme 4, Scheme 5, p.10-14
[34]Scheme 1
[35]Fig.1, p.32863-32864
[36]Fig.2, p.907-909
[37]Scheme 1
[38]Fig.1, p.4587-4588
[39]p.13891, p.13894-13896
[40]Fig.1b, p.41101-41105
[41]Fig.1, p.6834-6835
[42]p.13535-13537
[44]Fig.2, p.675-676
[45]Scheme 1, p.9912
[46]Fig.1, p.15734
[47]Scheme 1, Scheme 2, p.7558-7561
[48]Scheme 1, Scheme 2, Scheme 3, p.907-911
[49]Scheme 1, p.108-109
[50]Scheme 1, p.28233-28236
[51]p.971-972
[52]Scheme 1
[53]Fig.4, p.503-505, p.511-514

references
[1]
CommentsCHARACTERIZATION.
Medline ID74032505
PubMed ID4753764
JournalFEBS Lett
Year1973
Volume37
Pages82-8
AuthorsWeintraub H, Vincent F, Baulieu EE, Alfsen A
TitleMolecular weight determination and structural studies of Pseudomonas testosteroni delta 5 leads to 4-3-oxosteroid isomerase (EC 5.3.3.1).
Related UniProtKBP00947
[2]
PubMed ID6746641
JournalJ Biol Chem
Year1984
Volume259
Pages9096-103
AuthorsWestbrook EM, Piro OE, Sigler PB
TitleThe 6-A crystal structure of delta 5-3-ketosteroid isomerase. Architecture and location of the active center.
[3]
PubMed ID2888482
JournalBiochemistry
Year1987
Volume26
Pages3927-37
AuthorsKuliopulos A, Westbrook EM, Talalay P, Mildvan AS
TitlePositioning of a spin-labeled substrate analogue into the structure of delta 5-3-ketosteroid isomerase by combined kinetic, magnetic resonance, and X-ray diffraction methods.
[4]
PubMed ID2706241
JournalBiochemistry
Year1989
Volume28
Pages149-59
AuthorsKuliopulos A, Mildvan AS, Shortle D, Talalay P
TitleKinetic and ultraviolet spectroscopic studies of active-site mutants of delta 5-3-ketosteroid isomerase.
[5]
PubMed ID2271654
JournalBiochemistry
Year1990
Volume29
Pages10271-80
AuthorsKuliopulos A, Talalay P, Mildvan AS
TitleCombined effects of two mutations of catalytic residues on the ketosteroid isomerase reaction.
[6]
PubMed ID2223781
JournalBiochemistry
Year1990
Volume29
Pages7491-500
AuthorsXue LA, Talalay P, Mildvan AS
TitleStudies of the mechanism of the delta 5-3-ketosteroid isomerase reaction by substrate, solvent, and combined kinetic deuterium isotope effects on wild-type and mutant enzymes.
[7]
PubMed ID2009258
JournalBiochemistry
Year1991
Volume30
Pages3169-78
AuthorsKuliopulos A, Mullen GP, Xue L, Mildvan AS
TitleStereochemistry of the concerted enolization catalyzed by delta 5-3-ketosteroid isomerase.
[8]
PubMed ID2036366
JournalBiochemistry
Year1991
Volume30
Pages4991-7
AuthorsXue LA, Kuliopulos A, Mildvan AS, Talalay P
TitleCatalytic mechanism of an active-site mutant (D38N) of delta 5-3-ketosteroid isomerase. Direct spectroscopic evidence for dienol intermediates.
[9]
PubMed ID1932008
JournalBiochemistry
Year1991
Volume30
Pages10858-65
AuthorsXue LA, Talalay P, Mildvan AS
TitleStudies of the catalytic mechanism of an active-site mutant (Y14F) of delta 5-3-ketosteroid isomerase by kinetic deuterium isotope effects.
[10]
PubMed ID8093664
JournalBiochemistry
Year1993
Volume32
Pages694-8
AuthorsHawkinson DC, Pollack RM
TitleIs a proton relay involved in the mechanism of 3-oxo-delta 5-steroid isomerase?
[11]
PubMed ID8439542
JournalBiochemistry
Year1993
Volume32
Pages1816-24
AuthorsLi YK, Kuliopulos A, Mildvan AS, Talalay P
TitleEnvironments and mechanistic roles of the tyrosine residues of delta 5-3-ketosteroid isomerase.
[12]
PubMed ID8117732
JournalBiochemistry
Year1994
Volume33
Pages2682-7
AuthorsBrooks B, Benisek WF
TitleMechanism of the reaction catalyzed by delta 5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni: kinetic properties of a modified enzyme in which tyrosine 14 is replaced by 3-fluorotyrosine.
[13]
PubMed ID7918439
JournalBiochemistry
Year1994
Volume33
Pages12172-83
AuthorsHawkinson DC, Pollack RM, Ambulos NP Jr
TitleEvaluation of the internal equilibrium constant for 3-oxo-delta 5-steroid isomerase using the D38E and D38N mutants: the energetic basis for catalysis.
[14]
PubMed ID8117731
JournalBiochemistry
Year1994
Volume33
Pages2672-81
AuthorsHolman CM, Benisek WF
TitleExtent of proton transfer in the transition states of the reaction catalyzed by the delta 5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni: site-specific replacement of the active site base, aspartate 38, by the weaker base alanine-3-sulfinate.
[15]
PubMed ID7947798
JournalBiochemistry
Year1994
Volume33
Pages13896-902
AuthorsZawrotny ME, Pollack RM
TitleReaction energetics of a mutant 3-oxo-delta 5-steroid isomerase with an altered active site base (D38E).
[16]
PubMed ID7578024
JournalBiochemistry
Year1995
Volume34
Pages14245-53
AuthorsHolman CM, Benisek WF
TitleInsights into the catalytic mechanism and active-site environment of Comamonas testosteroni delta 5-3-ketosteroid isomerase as revealed by site-directed mutagenesis of the catalytic base aspartate-38.
[17]
PubMed ID7756287
JournalBiochemistry
Year1995
Volume34
Pages6562-72
AuthorsZhao Q, Li YK, Mildvan AS, Talalay P
TitleUltraviolet spectroscopic evidence for decreased motion of the active site tyrosine residue of delta 5-3-ketosteroid isomerase by steroid binding.
[18]
PubMed ID7730300
JournalJ Bacteriol
Year1995
Volume177
Pages2602-5
AuthorsKim SW, Choi KY
TitleIdentification of active site residues by site-directed mutagenesis of delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B.
[19]
PubMed ID7492546
JournalBiochemistry
Year1995
Volume34
Pages15453-8
AuthorsBrothers PN, Blotny G, Qi L, Pollack RM
TitleAn active site phenylalanine of 3-oxo-delta 5-steroid isomerase is catalytically important for proton transfer.
[20]
PubMed ID8639590
JournalBiochemistry
Year1996
Volume35
Pages6438-42
AuthorsZawrotny ME, Hawkinson DC, Blotny G, Pollack RM
TitleMechanism of proton transfer in the isomerization of 5-androstene-3, 17-dione by 3-oxo-delta 5-steroid isomerase and its D38E mutant.
[21]
PubMed ID8634283
JournalBiochemistry
Year1996
Volume35
Pages1525-32
AuthorsZhao Q, Abeygunawardana C, Mildvan AS
Title13C NMR relaxation studies of backbone and side chain motion of the catalytic tyrosine residue in free and steroid-bound delta 5-3-ketosteroid isomerase.
[22]
PubMed ID8710850
JournalProc Natl Acad Sci U S A
Year1996
Volume93
Pages8220-4
AuthorsZhao Q, Abeygunawardana C, Talalay P, Mildvan AS
TitleNMR evidence for the participation of a low-barrier hydrogen bond in the mechanism of delta 5-3-ketosteroid isomerase.
[23]
PubMed ID8859999
JournalProteins
Year1996
Volume24
Pages514-5
AuthorsOh BH, Kim SW, Ryu SE, Kim SS, Yoon MK, Choi KY
TitleCrystallization and preliminary x-ray crystallographic studies of ketosteroid isomerase from Pseudomonas putida biotype B.
[24]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID98039133
PubMed ID9369474
JournalBiochemistry
Year1997
Volume36
Pages14030-6
AuthorsKim SW, Cha SS, Cho HS, Kim JS, Ha NC, Cho MJ, Joo S, Kim KK, Choi KY, Oh BH
TitleHigh-resolution crystal structures of delta5-3-ketosteroid isomerase with and without a reaction intermediate analogue.
Related PDB4tsu,8cho,1oh0
Related UniProtKBP00947,P07445
[25]
PubMed ID9398180
JournalBiochemistry
Year1997
Volume36
Pages14616-26
AuthorsZhao Q, Abeygunawardana C, Gittis AG, Mildvan AS
TitleHydrogen bonding at the active site of delta 5-3-ketosteroid isomerase.
[26]
PubMed ID9131995
JournalBiochemistry
Year1997
Volume36
Pages3458-72
AuthorsZhao Q, Abeygunawardana C, Mildvan AS
TitleNMR studies of the secondary structure in solution and the steroid binding site of delta5-3-ketosteroid isomerase in complexes with diamagnetic and paramagnetic steroids.
[27]
PubMed ID9401033
JournalJ Bacteriol
Year1997
Volume179
Pages7742-7
AuthorsKim SW, Joo S, Choi G, Cho HS, Oh BH, Choi KY
TitleMutational analysis of the three cysteines and active-site aspartic acid 103 of ketosteroid isomerase from Pseudomonas putida biotype B.
[28]
PubMed ID9342312
JournalProc Natl Acad Sci U S A
Year1997
Volume94
Pages11773-6
AuthorsLin CH, Hoffman TZ, Wirsching P, Barbas CF 3rd, Janda KD, Lerner RA
TitleOn roads not taken in the evolution of protein catalysts: antibody steroid isomerases that use an enamine mechanism.
[29]
CommentsSTRUCTURE BY NMR.
Medline ID97258944
PubMed ID9103200
JournalScience
Year1997
Volume276
Pages415-8
AuthorsWu ZR, Ebrahimian S, Zawrotny ME, Thornburg LD, Perez-Alvarado GC, Brothers P, Pollack RM, Summers MF
TitleSolution structure of 3-oxo-delta5-steroid isomerase.
Related PDB1isk,1opy
Related UniProtKBP00947
[30]
PubMed ID9622484
JournalBiochemistry
Year1998
Volume37
Pages8325-30
AuthorsCho HS, Choi G, Choi KY, Oh BH
TitleCrystal structure and enzyme mechanism of Delta 5-3-ketosteroid isomerase from Pseudomonas testosteroni.
[31]
CommentsX-ray crystallography
PubMed ID9778345
JournalBiochemistry
Year1998
Volume37
Pages14701-12
AuthorsMassiah MA, Abeygunawardana C, Gittis AG, Mildvan AS
TitleSolution structure of Delta 5-3-ketosteroid isomerase complexed with the steroid 19-nortestosterone hemisuccinate.
Related PDB1buq
[32]
PubMed ID9578560
JournalBiochemistry
Year1998
Volume37
Pages6760-6
AuthorsQi L, Pollack RM
TitleCatalytic contribution of phenylalanine-101 of 3-oxo-Delta 5-steroid isomerase.
[33]
PubMed ID10496971
JournalArch Biochem Biophys
Year1999
Volume370
Pages9-15
AuthorsPollack RM, Thornburg LD, Wu ZR, Summers MF
TitleMechanistic insights from the three-dimensional structure of 3-oxo-Delta(5)-steroid isomerase.
[34]
CommentsX-ray crystallography
PubMed ID10529226
JournalBiochemistry
Year1999
Volume38
Pages13810-9
AuthorsKim DH, Nam GH, Jang DS, Choi G, Joo S, Kim JS, Oh BH, Choi KY
TitleRoles of active site aromatic residues in catalysis by ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB1c7h
[35]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID20020257
PubMed ID10551849
JournalJ Biol Chem
Year1999
Volume274
Pages32863-8
AuthorsCho HS, Ha NC, Choi G, Kim HJ, Lee D, Oh KS, Kim KS, Lee W, Choi KY, Oh BH
TitleCrystal structure of delta(5)-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with equilenin settles the correct hydrogen bonding scheme for transition state stabilization.
Related PDB1qjg
Related UniProtKBP00947
[36]
CommentsX-ray crystallography
PubMed ID10653633
JournalBiochemistry
Year2000
Volume39
Pages903-9
AuthorsChoi G, Ha NC, Kim SW, Kim DH, Park S, Oh BH, Choi KY
TitleAsp-99 donates a hydrogen bond not to Tyr-14 but to the steroid directly in the catalytic mechanism of Delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB1cqs
[37]
PubMed ID10727228
JournalBiochemistry
Year2000
Volume39
Pages3351-9
AuthorsHenot F, Pollack RM
TitleCatalytic activity of the D38A mutant of 3-oxo-Delta 5-steroid isomerase: recruitment of aspartate-99 as the base.
[38]
CommentsX-ray crystallography
PubMed ID10769113
JournalBiochemistry
Year2000
Volume39
Pages4581-9
AuthorsKim DH, Jang DS, Nam GH, Choi G, Kim JS, Ha NC, Kim MS, Oh BH, Choi KY
TitleContribution of the hydrogen-bond network involving a tyrosine triad in the active site to the structure and function of a highly proficient ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB1dmm,1dmn,1dmq
[39]
PubMed ID11076530
JournalBiochemistry
Year2000
Volume39
Pages13891-6
AuthorsOh KS, Cha SS, Kim DH, Cho HS, Ha NC, Choi G, Lee JY, Tarakeshwar P, Son HS, Choi KY, Oh BH, Kim KS
TitleRole of catalytic residues in enzymatic mechanisms of homologous ketosteroid isomerases.
[40]
CommentsX-ray crystallography
PubMed ID11007792
JournalJ Biol Chem
Year2000
Volume275
Pages41100-6
AuthorsHa NC, Kim MS, Lee W, Choi KY, Oh BH
TitleDetection of large pKa perturbations of an inhibitor and a catalytic group at an enzyme active site, a mechanistic basis for catalytic power of many enzymes.
Related PDB1e3r,1e3v,1ogx
[41]
CommentsX-ray crystallography
PubMed ID11389596
JournalBiochemistry
Year2001
Volume40
Pages6828-35
AuthorsChoi G, Ha NC, Kim MS, Hong BH, Oh BH, Choi KY
TitlePseudoreversion of the catalytic activity of Y14F by the additional substitution(s) of tyrosine with phenylalanine in the hydrogen bond network of delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB1e97,1ea2
[42]
CommentsX-ray crystallography
PubMed ID11695900
JournalBiochemistry
Year2001
Volume40
Pages13529-37
AuthorsNam GH, Jang DS, Cha SS, Lee TH, Kim DH, Hong BH, Yun YS, Oh BH, Choi KY
TitleMaintenance of alpha-helical structures by phenyl rings in the active-site tyrosine triad contributes to catalysis and stability of ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB1k41
[43]
PubMed ID11300777
JournalBiochemistry
Year2001
Volume40
Pages3967-73
AuthorsYun S, Jang DS, Kim DH, Choi KY, Lee HC
Title15N NMR relaxation studies of backbone dynamics in free and steroid-bound Delta 5-3-ketosteroid isomerase from Pseudomonas testosteroni.
[44]
PubMed ID11751047
JournalCurr Opin Struct Biol
Year2001
Volume11
Pages674-8
AuthorsHa NC, Choi G, Choi KY, Oh BH
TitleStructure and enzymology of Delta5-3-ketosteroid isomerase.
[45]
PubMed ID11583562
JournalJ Am Chem Soc
Year2001
Volume123
Pages9912-3
AuthorsThornburg LD, Goldfeder YR, Wilde TC, Pollack RM
TitleSelective catalysis of elementary steps by Asp-99 and Tyr-14 of 3-Oxo-delta(5)-steroid isomerase.
[46]
PubMed ID12501201
JournalBiochemistry
Year2002
Volume41
Pages15728-35
AuthorsFeierberg I, Aqvist J
TitleThe catalytic power of ketosteroid isomerase investigated by computer simulation.
[47]
PubMed ID12812495
JournalJ Am Chem Soc
Year2003
Volume125
Pages7553-61
AuthorsMazumder D, Kahn K, Bruice TC
TitleComputational study of ketosteroid isomerase: insights from molecular dynamics simulation of enzyme bound substrate and intermediate.
[48]
PubMed ID12537487
JournalJ Am Chem Soc
Year2003
Volume125
Pages901-11
AuthorsPark H, Merz KM Jr
TitleMolecular dynamics and quantum chemical studies on the catalytic mechanism of Delta5-3-ketosteroid isomerase: the catalytic diad versus the cooperative hydrogen bond mechanism.
[49]
PubMed ID12944376
JournalJ Biochem (Tokyo)
Year2003
Volume134
Pages101-10
AuthorsNam GH, Kim DH, Ha NC, Jang do S, Yun YS, Hong BH, Oh BH, Choi KY
TitleContribution of conserved amino acids at the dimeric interface to the conformational stability and the structural integrity of the active site in ketosteroid isomerase from Pseudomonas putida biotype B.
[50]
CommentsX-ray crystallography
PubMed ID12734184
JournalJ Biol Chem
Year2003
Volume278
Pages28229-36
AuthorsYun YS, Lee TH, Nam GH, Jang do S, Shin S, Oh BH, Choi KY
TitleOrigin of the different pH activity profile in two homologous ketosteroid isomerases.
Related PDB1ocv
[51]
PubMed ID15228388
JournalBiochem J
Year2004
Volume382
Pages967-73
AuthorsJang do S, Cha HJ, Cha SS, Hong BH, Ha NC, Lee JY, Oh BH, Lee HS, Choi KY
TitleStructural double-mutant cycle analysis of a hydrogen bond network in ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB1w00
[52]
PubMed ID15819891
JournalFEBS J
Year2005
Volume272
Pages1999-2011
AuthorsYun YS, Nam GH, Kim YG, Oh BH, Choi KY
TitleSmall exterior hydrophobic cluster contributes to conformational stability and steroid binding in ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB1w6y
[53]
PubMed ID16602823
JournalPLoS Biol
Year2006
Volume4
Pagese99
AuthorsKraut DA, Sigala PA, Pybus B, Liu CW, Ringe D, Petsko GA, Herschlag D
TitleTesting electrostatic complementarity in enzyme catalysis: hydrogen bonding in the ketosteroid isomerase oxyanion hole.
Related PDB2b32

comments
This enzyme is homologous to that from Pseudomonas putida (S00177 in EzCatDB). The only difference between these enzymes is the existence of the third tyrosine at the catalytic site in the counterpart enzyme.
This enzyme catalyzes the following reactions:
(A) Isomerization; Shift of double-bond position (from O=C-C to O-C=C), forming an enolic intermediate.
(B) Isomerization; Shift of double-bond position (from O-C=C-C=C to O=C-C=C-C)

createdupdated
2005-05-092009-03-19
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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