DB code: S00545

CATH domain 3.10.450.50 : Nuclear Transport Factor 2; Chain Catalytic domain
E.C. 5.3.3.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.10.450.50 : Nuclear Transport Factor 2; Chain S00176 S00177 T00024

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P00947 Steroid Delta-isomerase
EC 5.3.3.1
Delta(5)-3-ketosteroid isomerase
PF02136 (NTF2)
[Graphical View]

KEGG enzyme name
steroid 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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00947 SDIS_COMTE A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)- steroid. Homodimer.

KEGG Pathways
Map code Pathways E.C.
MAP00140 C21-Steroid hormone metabolism
MAP00150 Androgen and estrogen metabolism

Compound table
Substrates Products Intermediates
KEGG-id C01034 C00619 I00017
E.C.
Compound 3-Oxo-delta5-steroid 3-Oxo-delta4-steroid 3-Hydroxy-androsta-3,5-dien
Type carbohydrate,steroid carbohydrate,steroid
ChEBI 47909
PubChem 439372
439274
1buqA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:NTH Unbound
1buqB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:NTH Unbound
1iskA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1iskB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ocvA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ocvB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ocvC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ocvD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ogzA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:EQU
1ohpA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:ESR Unbound Unbound
1ohpB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:ESR Unbound Unbound
1ohpC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:ESR Unbound Unbound
1ohpD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:ESR Unbound Unbound
1ohsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:5SD Unbound Unbound
1ohsB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:5SD Unbound Unbound
1ohsC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:5SD Unbound Unbound
1ohsD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qjgA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:EQU
1qjgB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:EQU
1qjgC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:EQU
1qjgD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:EQU
1qjgE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:EQU
1qjgF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:EQU
8choA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [38], [41]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1buqA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14;ASP 38; ;ASP 99 mutant Y55F, Y88F
1buqB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 214;ASP 238;;ASP 299 mutant Y255F, Y288F
1iskA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14;ASP 38;TYR 55;ASP 99
1iskB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14;ASP 38;TYR 55;ASP 99
1ocvA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14;ASP 38;TYR 55;ASP 99 mutant T83I, F116W
1ocvB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 214;ASP 238;TYR 255;ASP 299 mutant T283I, F316W
1ocvC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 414;ASP 438;TYR 455;ASP 499 mutant T483I, F516W
1ocvD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 614;ASP 638;TYR 655;ASP 699 mutant T683I, F716W
1ogzA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14;ASP 38;TYR 55;ASP 99 mutant P39A, T83I
1ohpA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14; ;TYR 55;ASP 99 mutant D38N, T83I
1ohpB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 214;;TYR 255;ASP 299 mutant D238N, T283I
1ohpC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14; ;TYR 55;ASP 99 mutant D38N, T83I
1ohpD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 214;;TYR 255;ASP 299 mutant D238N, T283I
1ohsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ; ;TYR 55;ASP 99 mutant Y14F, D38N, T83I
1ohsB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ; ;TYR 255;ASP 299 mutant Y214F, D238N, T283I
1ohsC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ; ;TYR 55;ASP 99 mutant Y14F, D38N, T83I
1ohsD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ; ;TYR 255;ASP 299 mutant Y214F, D238N, T283I
1qjgA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14; ;TYR 55;ASP 99 mutant D38N, T83I
1qjgB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14; ;TYR 55;ASP 99 mutant D38N, T83I
1qjgC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14; ;TYR 55;ASP 99 mutant D38N, T83I
1qjgD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14; ;TYR 55;ASP 99 mutant D38N, T83I
1qjgE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14; ;TYR 55;ASP 99 mutant D38N, T83I
1qjgF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14; ;TYR 55;ASP 99 mutant D38N, T83I
8choA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 14;ASP 38;TYR 55;ASP 99 mutant T83I

References for Catalytic Mechanism
References Sections No. 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]
Resource
Comments CHARACTERIZATION.
Medline ID 74032505
PubMed ID 4753764
Journal FEBS Lett
Year 1973
Volume 37
Pages 82-8
Authors Weintraub H, Vincent F, Baulieu EE, Alfsen A
Title Molecular weight determination and structural studies of Pseudomonas testosteroni delta 5 leads to 4-3-oxosteroid isomerase (EC 5.3.3.1).
Related PDB
Related UniProtKB P00947
[2]
Resource
Comments
Medline ID
PubMed ID 6746641
Journal J Biol Chem
Year 1984
Volume 259
Pages 9096-103
Authors Westbrook EM, Piro OE, Sigler PB
Title The 6-A crystal structure of delta 5-3-ketosteroid isomerase. Architecture and location of the active center.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 2888482
Journal Biochemistry
Year 1987
Volume 26
Pages 3927-37
Authors Kuliopulos A, Westbrook EM, Talalay P, Mildvan AS
Title Positioning 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.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 2706241
Journal Biochemistry
Year 1989
Volume 28
Pages 149-59
Authors Kuliopulos A, Mildvan AS, Shortle D, Talalay P
Title Kinetic and ultraviolet spectroscopic studies of active-site mutants of delta 5-3-ketosteroid isomerase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 2271654
Journal Biochemistry
Year 1990
Volume 29
Pages 10271-80
Authors Kuliopulos A, Talalay P, Mildvan AS
Title Combined effects of two mutations of catalytic residues on the ketosteroid isomerase reaction.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 2223781
Journal Biochemistry
Year 1990
Volume 29
Pages 7491-500
Authors Xue LA, Talalay P, Mildvan AS
Title Studies 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.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 2009258
Journal Biochemistry
Year 1991
Volume 30
Pages 3169-78
Authors Kuliopulos A, Mullen GP, Xue L, Mildvan AS
Title Stereochemistry of the concerted enolization catalyzed by delta 5-3-ketosteroid isomerase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 2036366
Journal Biochemistry
Year 1991
Volume 30
Pages 4991-7
Authors Xue LA, Kuliopulos A, Mildvan AS, Talalay P
Title Catalytic mechanism of an active-site mutant (D38N) of delta 5-3-ketosteroid isomerase. Direct spectroscopic evidence for dienol intermediates.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 1932008
Journal Biochemistry
Year 1991
Volume 30
Pages 10858-65
Authors Xue LA, Talalay P, Mildvan AS
Title Studies of the catalytic mechanism of an active-site mutant (Y14F) of delta 5-3-ketosteroid isomerase by kinetic deuterium isotope effects.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8093664
Journal Biochemistry
Year 1993
Volume 32
Pages 694-8
Authors Hawkinson DC, Pollack RM
Title Is a proton relay involved in the mechanism of 3-oxo-delta 5-steroid isomerase?
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 8439542
Journal Biochemistry
Year 1993
Volume 32
Pages 1816-24
Authors Li YK, Kuliopulos A, Mildvan AS, Talalay P
Title Environments and mechanistic roles of the tyrosine residues of delta 5-3-ketosteroid isomerase.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 8117732
Journal Biochemistry
Year 1994
Volume 33
Pages 2682-7
Authors Brooks B, Benisek WF
Title Mechanism 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.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 7918439
Journal Biochemistry
Year 1994
Volume 33
Pages 12172-83
Authors Hawkinson DC, Pollack RM, Ambulos NP Jr
Title Evaluation of the internal equilibrium constant for 3-oxo-delta 5-steroid isomerase using the D38E and D38N mutants: the energetic basis for catalysis.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 8117731
Journal Biochemistry
Year 1994
Volume 33
Pages 2672-81
Authors Holman CM, Benisek WF
Title Extent 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.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 7947798
Journal Biochemistry
Year 1994
Volume 33
Pages 13896-902
Authors Zawrotny ME, Pollack RM
Title Reaction energetics of a mutant 3-oxo-delta 5-steroid isomerase with an altered active site base (D38E).
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 7578024
Journal Biochemistry
Year 1995
Volume 34
Pages 14245-53
Authors Holman CM, Benisek WF
Title Insights 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.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 7756287
Journal Biochemistry
Year 1995
Volume 34
Pages 6562-72
Authors Zhao Q, Li YK, Mildvan AS, Talalay P
Title Ultraviolet spectroscopic evidence for decreased motion of the active site tyrosine residue of delta 5-3-ketosteroid isomerase by steroid binding.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 7730300
Journal J Bacteriol
Year 1995
Volume 177
Pages 2602-5
Authors Kim SW, Choi KY
Title Identification of active site residues by site-directed mutagenesis of delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 7492546
Journal Biochemistry
Year 1995
Volume 34
Pages 15453-8
Authors Brothers PN, Blotny G, Qi L, Pollack RM
Title An active site phenylalanine of 3-oxo-delta 5-steroid isomerase is catalytically important for proton transfer.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 8639590
Journal Biochemistry
Year 1996
Volume 35
Pages 6438-42
Authors Zawrotny ME, Hawkinson DC, Blotny G, Pollack RM
Title Mechanism of proton transfer in the isomerization of 5-androstene-3, 17-dione by 3-oxo-delta 5-steroid isomerase and its D38E mutant.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 8634283
Journal Biochemistry
Year 1996
Volume 35
Pages 1525-32
Authors Zhao Q, Abeygunawardana C, Mildvan AS
Title 13C NMR relaxation studies of backbone and side chain motion of the catalytic tyrosine residue in free and steroid-bound delta 5-3-ketosteroid isomerase.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 8710850
Journal Proc Natl Acad Sci U S A
Year 1996
Volume 93
Pages 8220-4
Authors Zhao Q, Abeygunawardana C, Talalay P, Mildvan AS
Title NMR evidence for the participation of a low-barrier hydrogen bond in the mechanism of delta 5-3-ketosteroid isomerase.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 8859999
Journal Proteins
Year 1996
Volume 24
Pages 514-5
Authors Oh BH, Kim SW, Ryu SE, Kim SS, Yoon MK, Choi KY
Title Crystallization and preliminary x-ray crystallographic studies of ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB
Related UniProtKB
[24]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID 98039133
PubMed ID 9369474
Journal Biochemistry
Year 1997
Volume 36
Pages 14030-6
Authors Kim SW, Cha SS, Cho HS, Kim JS, Ha NC, Cho MJ, Joo S, Kim KK, Choi KY, Oh BH
Title High-resolution crystal structures of delta5-3-ketosteroid isomerase with and without a reaction intermediate analogue.
Related PDB 4tsu 8cho 1oh0
Related UniProtKB P00947 P07445
[25]
Resource
Comments
Medline ID
PubMed ID 9398180
Journal Biochemistry
Year 1997
Volume 36
Pages 14616-26
Authors Zhao Q, Abeygunawardana C, Gittis AG, Mildvan AS
Title Hydrogen bonding at the active site of delta 5-3-ketosteroid isomerase.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 9131995
Journal Biochemistry
Year 1997
Volume 36
Pages 3458-72
Authors Zhao Q, Abeygunawardana C, Mildvan AS
Title NMR studies of the secondary structure in solution and the steroid binding site of delta5-3-ketosteroid isomerase in complexes with diamagnetic and paramagnetic steroids.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 9401033
Journal J Bacteriol
Year 1997
Volume 179
Pages 7742-7
Authors Kim SW, Joo S, Choi G, Cho HS, Oh BH, Choi KY
Title Mutational analysis of the three cysteines and active-site aspartic acid 103 of ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 9342312
Journal Proc Natl Acad Sci U S A
Year 1997
Volume 94
Pages 11773-6
Authors Lin CH, Hoffman TZ, Wirsching P, Barbas CF 3rd, Janda KD, Lerner RA
Title On roads not taken in the evolution of protein catalysts: antibody steroid isomerases that use an enamine mechanism.
Related PDB
Related UniProtKB
[29]
Resource
Comments STRUCTURE BY NMR.
Medline ID 97258944
PubMed ID 9103200
Journal Science
Year 1997
Volume 276
Pages 415-8
Authors Wu ZR, Ebrahimian S, Zawrotny ME, Thornburg LD, Perez-Alvarado GC, Brothers P, Pollack RM, Summers MF
Title Solution structure of 3-oxo-delta5-steroid isomerase.
Related PDB 1isk 1opy
Related UniProtKB P00947
[30]
Resource
Comments
Medline ID
PubMed ID 9622484
Journal Biochemistry
Year 1998
Volume 37
Pages 8325-30
Authors Cho HS, Choi G, Choi KY, Oh BH
Title Crystal structure and enzyme mechanism of Delta 5-3-ketosteroid isomerase from Pseudomonas testosteroni.
Related PDB
Related UniProtKB
[31]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9778345
Journal Biochemistry
Year 1998
Volume 37
Pages 14701-12
Authors Massiah MA, Abeygunawardana C, Gittis AG, Mildvan AS
Title Solution structure of Delta 5-3-ketosteroid isomerase complexed with the steroid 19-nortestosterone hemisuccinate.
Related PDB 1buq
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 9578560
Journal Biochemistry
Year 1998
Volume 37
Pages 6760-6
Authors Qi L, Pollack RM
Title Catalytic contribution of phenylalanine-101 of 3-oxo-Delta 5-steroid isomerase.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 10496971
Journal Arch Biochem Biophys
Year 1999
Volume 370
Pages 9-15
Authors Pollack RM, Thornburg LD, Wu ZR, Summers MF
Title Mechanistic insights from the three-dimensional structure of 3-oxo-Delta(5)-steroid isomerase.
Related PDB
Related UniProtKB
[34]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10529226
Journal Biochemistry
Year 1999
Volume 38
Pages 13810-9
Authors Kim DH, Nam GH, Jang DS, Choi G, Joo S, Kim JS, Oh BH, Choi KY
Title Roles of active site aromatic residues in catalysis by ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB 1c7h
Related UniProtKB
[35]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID 20020257
PubMed ID 10551849
Journal J Biol Chem
Year 1999
Volume 274
Pages 32863-8
Authors Cho HS, Ha NC, Choi G, Kim HJ, Lee D, Oh KS, Kim KS, Lee W, Choi KY, Oh BH
Title Crystal 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 PDB 1qjg
Related UniProtKB P00947
[36]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10653633
Journal Biochemistry
Year 2000
Volume 39
Pages 903-9
Authors Choi G, Ha NC, Kim SW, Kim DH, Park S, Oh BH, Choi KY
Title Asp-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 PDB 1cqs
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 10727228
Journal Biochemistry
Year 2000
Volume 39
Pages 3351-9
Authors Henot F, Pollack RM
Title Catalytic activity of the D38A mutant of 3-oxo-Delta 5-steroid isomerase: recruitment of aspartate-99 as the base.
Related PDB
Related UniProtKB
[38]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10769113
Journal Biochemistry
Year 2000
Volume 39
Pages 4581-9
Authors Kim DH, Jang DS, Nam GH, Choi G, Kim JS, Ha NC, Kim MS, Oh BH, Choi KY
Title Contribution 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 PDB 1dmm 1dmn 1dmq
Related UniProtKB
[39]
Resource
Comments
Medline ID
PubMed ID 11076530
Journal Biochemistry
Year 2000
Volume 39
Pages 13891-6
Authors Oh KS, Cha SS, Kim DH, Cho HS, Ha NC, Choi G, Lee JY, Tarakeshwar P, Son HS, Choi KY, Oh BH, Kim KS
Title Role of catalytic residues in enzymatic mechanisms of homologous ketosteroid isomerases.
Related PDB
Related UniProtKB
[40]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11007792
Journal J Biol Chem
Year 2000
Volume 275
Pages 41100-6
Authors Ha NC, Kim MS, Lee W, Choi KY, Oh BH
Title Detection 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 PDB 1e3r 1e3v 1ogx
Related UniProtKB
[41]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11389596
Journal Biochemistry
Year 2001
Volume 40
Pages 6828-35
Authors Choi G, Ha NC, Kim MS, Hong BH, Oh BH, Choi KY
Title Pseudoreversion 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 PDB 1e97 1ea2
Related UniProtKB
[42]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11695900
Journal Biochemistry
Year 2001
Volume 40
Pages 13529-37
Authors Nam GH, Jang DS, Cha SS, Lee TH, Kim DH, Hong BH, Yun YS, Oh BH, Choi KY
Title Maintenance 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 PDB 1k41
Related UniProtKB
[43]
Resource
Comments
Medline ID
PubMed ID 11300777
Journal Biochemistry
Year 2001
Volume 40
Pages 3967-73
Authors Yun S, Jang DS, Kim DH, Choi KY, Lee HC
Title 15N NMR relaxation studies of backbone dynamics in free and steroid-bound Delta 5-3-ketosteroid isomerase from Pseudomonas testosteroni.
Related PDB
Related UniProtKB
[44]
Resource
Comments
Medline ID
PubMed ID 11751047
Journal Curr Opin Struct Biol
Year 2001
Volume 11
Pages 674-8
Authors Ha NC, Choi G, Choi KY, Oh BH
Title Structure and enzymology of Delta5-3-ketosteroid isomerase.
Related PDB
Related UniProtKB
[45]
Resource
Comments
Medline ID
PubMed ID 11583562
Journal J Am Chem Soc
Year 2001
Volume 123
Pages 9912-3
Authors Thornburg LD, Goldfeder YR, Wilde TC, Pollack RM
Title Selective catalysis of elementary steps by Asp-99 and Tyr-14 of 3-Oxo-delta(5)-steroid isomerase.
Related PDB
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 12501201
Journal Biochemistry
Year 2002
Volume 41
Pages 15728-35
Authors Feierberg I, Aqvist J
Title The catalytic power of ketosteroid isomerase investigated by computer simulation.
Related PDB
Related UniProtKB
[47]
Resource
Comments
Medline ID
PubMed ID 12812495
Journal J Am Chem Soc
Year 2003
Volume 125
Pages 7553-61
Authors Mazumder D, Kahn K, Bruice TC
Title Computational study of ketosteroid isomerase: insights from molecular dynamics simulation of enzyme bound substrate and intermediate.
Related PDB
Related UniProtKB
[48]
Resource
Comments
Medline ID
PubMed ID 12537487
Journal J Am Chem Soc
Year 2003
Volume 125
Pages 901-11
Authors Park H, Merz KM Jr
Title Molecular dynamics and quantum chemical studies on the catalytic mechanism of Delta5-3-ketosteroid isomerase: the catalytic diad versus the cooperative hydrogen bond mechanism.
Related PDB
Related UniProtKB
[49]
Resource
Comments
Medline ID
PubMed ID 12944376
Journal J Biochem (Tokyo)
Year 2003
Volume 134
Pages 101-10
Authors Nam GH, Kim DH, Ha NC, Jang do S, Yun YS, Hong BH, Oh BH, Choi KY
Title Contribution 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.
Related PDB
Related UniProtKB
[50]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12734184
Journal J Biol Chem
Year 2003
Volume 278
Pages 28229-36
Authors Yun YS, Lee TH, Nam GH, Jang do S, Shin S, Oh BH, Choi KY
Title Origin of the different pH activity profile in two homologous ketosteroid isomerases.
Related PDB 1ocv
Related UniProtKB
[51]
Resource
Comments
Medline ID
PubMed ID 15228388
Journal Biochem J
Year 2004
Volume 382
Pages 967-73
Authors Jang do S, Cha HJ, Cha SS, Hong BH, Ha NC, Lee JY, Oh BH, Lee HS, Choi KY
Title Structural double-mutant cycle analysis of a hydrogen bond network in ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB 1w00
Related UniProtKB
[52]
Resource
Comments
Medline ID
PubMed ID 15819891
Journal FEBS J
Year 2005
Volume 272
Pages 1999-2011
Authors Yun YS, Nam GH, Kim YG, Oh BH, Choi KY
Title Small exterior hydrophobic cluster contributes to conformational stability and steroid binding in ketosteroid isomerase from Pseudomonas putida biotype B.
Related PDB 1w6y
Related UniProtKB
[53]
Resource
Comments
Medline ID
PubMed ID 16602823
Journal PLoS Biol
Year 2006
Volume 4
Pages e99
Authors Kraut DA, Sigala PA, Pybus B, Liu CW, Ringe D, Petsko GA, Herschlag D
Title Testing electrostatic complementarity in enzyme catalysis: hydrogen bonding in the ketosteroid isomerase oxyanion hole.
Related PDB 2b32
Related UniProtKB

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)

Created Updated
2005-05-09 2009-03-19