DB code: S00177

CATH domain	3.10.450.50 : Nuclear Transport Factor 2; Chain	Catalytic domain
E.C.	5.3.3.1
CSA	1e3v 1vzz
M-CSA	1e3v 1vzz
MACiE

CATH domain	Related DB codes (homologues)
3.10.450.50 : Nuclear Transport Factor 2; Chain	S00176 S00545 T00024

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	Pfam
P07445	Steroid Delta-isomerase	EC 5.3.3.1 Delta(5)-3-ketosteroid isomerase	PF02136 (NTF2) PF12680 (SnoaL_2) [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
P07445	SDIS_PSEPU	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 47909
PubChem	439372 439372	439274 439274

1c7hA	Unbound	Unbound	Unbound
1cqsA	Unbound	Unbound	Intermediate-analogue:EQU
1cqsB	Unbound	Unbound	Intermediate-analogue:EQU
1dmmA	Unbound	Unbound	Unbound
1dmnA	Unbound	Unbound	Unbound
1dmqA	Unbound	Unbound	Unbound
1e3rA	Analogue:AND	Unbound	Unbound
1e3rB	Analogue:AND	Unbound	Unbound
1e3vA	Analogue:DXC	Unbound	Unbound
1e3vB	Analogue:DXC	Unbound	Unbound
1e97A	Unbound	Unbound	Unbound
1ea2A	Unbound	Unbound	Unbound
1gs3A	Unbound	Unbound	Intermediate-analogue:EQU
1k41A	Unbound	Unbound	Unbound
1k41B	Unbound	Unbound	Unbound
1ogxA	Unbound	Unbound	Intermediate-analogue:EQU
1ogxB	Unbound	Unbound	Intermediate-analogue:EQU
1oh0A	Unbound	Unbound	Intermediate-analogue:EQU
1oh0B	Unbound	Unbound	Intermediate-analogue:EQU
1ohoA	Unbound	Unbound	Intermediate-analogue:EQU
1opyA	Unbound	Unbound	Unbound
1vzzA	Unbound	Unbound	Unbound
1vzzB	Unbound	Unbound	Unbound
1w00A	Unbound	Unbound	Unbound
1w00B	Unbound	Unbound	Unbound
1w01A	Unbound	Unbound	Unbound
1w01B	Unbound	Unbound	Unbound
1w02A	Unbound	Unbound	Unbound
1w6yA	Unbound	Unbound	Intermediate-analogue:EQU
2b32A	Unbound	Unbound	Unbound
2b32B	Unbound	Unbound	Unbound
2b32C	Unbound	Unbound	Unbound
2b32D	Unbound	Unbound	Unbound
4tsuA	Unbound	Unbound	Intermediate-analogue:EQU
4tsuB	Unbound	Unbound	Intermediate-analogue:EQU

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

1c7hA	TYR 16;TYR 32;ASP 40;TYR 57;ASP 103				mutant R75A, invisible 62-64
1cqsA	TYR 16;TYR 32; ;TYR 57;				mutant D40N, D103E, invisible 63-64
1cqsB	TYR 216;TYR 232;;TYR 257;				mutant D240N, D303E, invisible 263-264
1dmmA	TYR 16;TYR 32;ASP 40; ;ASP 103				mutant Y57F, invisible 62-64
1dmnA	TYR 16; ;ASP 40; ;ASP 103				mutant Y32F, Y57F, invisible 62-64
1dmqA	TYR 16; ;ASP 40;TYR 57;ASP 103				mutant Y32F, invisible 62-64
1e3rA	TYR 16;TYR 32; ;TYR 57;ASP 103				mutant D40N
1e3rB	TYR 16;TYR 32; ;TYR 57;ASP 103				mutant D40N
1e3vA	TYR 16;TYR 32;ASP 40;TYR 57;ASP 103
1e3vB	TYR 16;TYR 32;ASP 40;TYR 57;ASP 103
1e97A	; ;ASP 40; ;ASP 103				mutant Y16F, Y32F, Y57F, invisible 62-64
1ea2A	;TYR 32;ASP 40;TYR 57;ASP 103				mutant Y16F, invisible 62-64
1gs3A	TYR 16; ; ; ;ASP 103				mutant Y32F, D40N, Y57F, Y119F, invisible 62-64
1k41A	TYR 16;TYR 32;ASP 40; ;ASP 103				mutant Y57S, invisible 61-64
1k41B	TYR 216;TYR 232;ASP 240;;ASP 303				mutant Y257S, invisible 261-264
1ogxA	TYR 16;TYR 32; ;TYR 57;ASP 103				mutant D40N
1ogxB	TYR 216;TYR 232;;TYR 257;ASP 303				mutant D240N
1oh0A	TYR 16;TYR 32;ASP 40;TYR 57;ASP 103
1oh0B	TYR 216;TYR 232;ASP 240;TYR 257;ASP 303
1ohoA	;TYR 32; ;TYR 57;ASP 103				mutant Y16F, D40N, invisible 62-64
1opyA	TYR 16;TYR 32;ASP 40;TYR 57;ASP 103
1vzzA	TYR 16; ;ASP 40;TYR 57;				mutant Y32F, D103L, invisible 63-64, 92-95
1vzzB	TYR 16; ;ASP 40;TYR 57;				mutant Y32F, D103L, invisible 63-64
1w00A	TYR 16;TYR 32;ASP 40;TYR 57;				mutant D103L, invisible 63-64
1w00B	TYR 16;TYR 32;ASP 40;TYR 57;				mutant D103L, invisible 63-64
1w01A	TYR 16;TYR 32;ASP 40; ;				mutant Y57F, D103L
1w01B	TYR 216;TYR 232;ASP 240; ;				mutant Y257F, D303L
1w02A	;TYR 32;ASP 40;TYR 57;				mutant Y16F, D103L, invisible 62-64, 92-95
1w6yA	TYR 16;TYR 32;ASP 40;TYR 57;ASP 103				mutant W92A, invisible 64
2b32A	TYR 16;TYR 32; ;TYR 57;ASP 103				mutant D40N, invisible 62-64
2b32B	TYR 16;TYR 32; ;TYR 57;ASP 103				mutant D40N, invisible 62-64
2b32C	TYR 16;TYR 32; ;TYR 57;ASP 103				mutant D40N, invisible 62-64
2b32D	TYR 16;TYR 32; ;TYR 57;ASP 103				mutant D40N, invisible 62-64
4tsuA	TYR 16;TYR 32;ASP 40;TYR 57;ASP 103
4tsuB	TYR 16;TYR 32;ASP 40;TYR 57;ASP 103

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 Comamonas testosteroni (S00545 in EzCatDB). The only difference between these enzymes is the existence of the third tyrosine at the catalytic site in this 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)

Comments

This enzyme is homologous to that from Comamonas testosteroni (S00545 in EzCatDB). The only difference between these enzymes is the existence of the third tyrosine at the catalytic site in this 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