EzCatDB: D00264

DB codeD00264
CATH domainDomain 13.40.50.1100
Domain 23.40.50.1100Catalytic domain
E.C.2.5.1.47
CSA1oas

CATH domainRelated DB codes (homologues)
3.40.50.1100T00088,T00089

Enzyme Name
Swiss-protKEGG

P0A1E3
Protein nameCysteine synthase Acysteine synthase
O-acetyl-L-serine sulfhydrylase
O-acetyl-L-serine sulfohydrolase
O-acetylserine (thiol)-lyase
O-acetylserine (thiol)-lyase A
O-acetylserine sulfhydrylase
O3-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide)
acetylserine sulfhydrylase
cysteine synthetase
S-sulfocysteine synthase
3-O-acetyl-L-serine:hydrogen-sulfide2-amino-2-carboxyethyltransferase
SynonymsEC 2.5.1.47
O-acetylserine sulfhydrylase A
CSase A
O-acetylserine (Thiol)-lyase A

KEGG pathways
MAP codePathways
MAP00272Cysteine metabolism
MAP00450Selenoamino acid metabolism
MAP00920Sulfur metabolism

Swiss-prot:Accession NumberP0A1E3
Entry nameCYSK_SALTY
ActivityO(3)-acetyl-L-serine + H(2)S = L-cysteine + acetate.
SubunitHomodimer.
Subcellular location
CofactorPyridoxal phosphate.


CofactorsSubstratesProductsintermediates
KEGG-idC00018C00979C00283C00097C00033
CompoundPyridoxal phosphateO3-Acetyl-L-serineHydrogen sulfideL-CysteineAcetate
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionamino acids,carbohydratesulfhydryl groupamino acids,sulfhydryl groupcarboxyl group
1d6sA01UnboundUnboundUnboundUnboundUnboundUnbound
1d6sB01UnboundUnboundUnboundUnboundUnboundUnbound
1fcjA01UnboundUnboundUnboundUnboundUnboundUnbound
1fcjB01UnboundUnboundUnboundUnboundUnboundUnbound
1fcjC01UnboundUnboundUnboundUnboundUnboundUnbound
1fcjD01UnboundUnboundUnboundUnboundUnboundUnbound
1oasA01UnboundUnboundUnboundUnboundUnboundUnbound
1oasB01UnboundUnboundUnboundUnboundUnboundUnbound
1d6sA02Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:MET-PLP
1d6sB02Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-MET
1fcjA02Bound:PLPUnboundAnalogue:SO4UnboundUnboundUnbound
1fcjB02Bound:PLPUnboundAnalogue:SO4UnboundUnboundUnbound
1fcjC02Bound:PLPUnboundAnalogue:SO4UnboundUnboundUnbound
1fcjD02Bound:PLPUnboundAnalogue:SO4UnboundUnboundUnbound
1oasA02Bound:PLPUnboundUnboundUnboundUnboundUnbound
1oasB02Bound:PLPUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1oas & literature [9] & [19]
pdbCatalytic residuesCofactor-binding residuescomment
1d6sA01
ARG 34;ILE 267;LEU 268(Allosteric anion-binding site)

1d6sB01
ARG 34;ILE 267;LEU 268(Allosteric anion-binding site)

1fcjA01
ARG 34;ILE 267;LEU 268(Allosteric anion-binding site)

1fcjB01
ARG 34;ILE 267;LEU 268(Allosteric anion-binding site)

1fcjC01
ARG 34;ILE 267;LEU 268(Allosteric anion-binding site)

1fcjD01
ARG 34;ILE 267;LEU 268(Allosteric anion-binding site)

1oasA01
ARG 34;ILE 267;LEU 268(Allosteric anion-binding site)

1oasB01
ARG 34;ILE 267;LEU 268(Allosteric anion-binding site)

1d6sA02      

mutant K41A
1d6sB02      

mutant K41A
1fcjA02LYS 41


1fcjB02LYS 41


1fcjC02LYS 41


1fcjD02LYS 41


1oasA02LYS 41


1oasB02LYS 41



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Scheme I, p.2301-23036
[6]Scheme 1, Scheme 3
[7]Scheme 3p.12319-12320, p.12321
[8]Scheme 4A, p.6364, Scheme 5
[9]

[10]Scheme 1, p.4780-47827
[12]Scheme 1, p.15424-154276
[13]Scheme 1, p.126-1285
[14]Scheme 14
[16]Scheme 1, Scheme 2, p.946-949
[19]p.283-284

references
[1]
PubMed ID398768
JournalCiba Found Symp
Year1979
Volume(72)
Pages87-99
AuthorsKredich NM, Hulanicka MD, Hallquist SG
TitleSynthesis of L-cysteine in Salmonella typhimurium.
[2]
PubMed ID1540585
JournalBiochemistry
Year1992
Volume31
Pages2298-303
AuthorsCook PF, Hara S, Nalabolu S, Schnackerz KD
TitlepH dependence of the absorbance and 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine.
[3]
PubMed ID8518286
JournalBiochemistry
Year1993
Volume32
Pages6433-42
AuthorsTai CH, Nalabolu SR, Jacobson TM, Minter DE, Cook PF
TitleKinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants.
[4]
PubMed ID8515470
JournalJ Mol Biol
Year1993
Volume231
Pages1130-2
AuthorsRao GS, Mottonen J, Goldsmith EJ, Cook PF
TitleCrystallization and preliminary X-ray data for the A-isozyme of O-acetylserine sulfhydrylase from Salmonella typhimurium.
[5]
PubMed ID7503562
JournalArch Biochem Biophys
Year1995
Volume324
Pages71-7
AuthorsSchnackerz KD, Cook PF
TitleResolution of pyridoxal 5'-phosphate from O-acetylserine sulfhydrylase from Salmonella typhimurium and reconstitution of apoenzyme with cofactor and cofactor analogues as a probe of the cofactor binding site.
[6]
PubMed ID7547955
JournalBiochemistry
Year1995
Volume34
Pages12152-60
AuthorsSchnackerz KD, Tai CH, Simmons JW 3rd, Jacobson TM, Rao GS, Cook PF
TitleIdentification and spectral characterization of the external aldimine of the O-acetylserine sulfhydrylase reaction.
[7]
PubMed ID7547974
JournalBiochemistry
Year1995
Volume34
Pages12311-22
AuthorsTai CH, Nalabolu SR, Simmons JW 3rd, Jacobson TM, Cook PF
TitleAcid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studies.
[8]
PubMed ID8639581
JournalBiochemistry
Year1996
Volume35
Pages6358-65
AuthorsHwang CC, Woehl EU, Minter DE, Dunn MF, Cook PF
TitleKinetic isotope effects as a probe of the beta-elimination reaction catalyzed by O-acetylserine sulfhydrylase.
[9]
PubMed ID8873618
JournalBiochemistry
Year1996
Volume35
Pages13485-93
AuthorsRege VD, Kredich NM, Tai CH, Karsten WE, Schnackerz KD, Cook PF
TitleA change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst.
[10]
PubMed ID8664267
JournalBiochemistry
Year1996
Volume35
Pages4776-83
AuthorsWoehl EU, Tai CH, Dunn MF, Cook PF
TitleFormation of the alpha-aminoacrylate immediate limits the overall reaction catalyzed by O-acetylserine sulfhydrylase.
[11]
PubMed ID8617276
JournalEur J Biochem
Year1996
Volume236
Pages272-82
AuthorsRolland N, Ruffet ML, Job D, Douce R, Droux M
TitleSpinach chloroplast 0-acetylserine (thiol)-lyase exhibits two catalytically non-equivalent pyridoxal-5'-phosphate-containing active sites.
[12]
PubMed ID9398272
JournalBiochemistry
Year1997
Volume36
Pages15419-27
AuthorsBenci S, Vaccari S, Mozzarelli A, Cook PF
TitleTime-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates.
[13]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND REVISIONS TO 266-267.
Medline ID98437375
PubMed ID9761678
JournalJ Mol Biol
Year1998
Volume283
Pages121-33
AuthorsBurkhard P, Rao GS, Hohenester E, Schnackerz KD, Cook PF, Jansonius JN
TitleThree-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium.
Related PDB1oas
Related Swiss-protP0A1E3
[14]
PubMed ID9761679
JournalJ Mol Biol
Year1998
Volume283
Pages135-46
AuthorsMozzarelli A, Bettati S, Pucci AM, Burkhard P, Cook PF
TitleCatalytic competence of O-acetylserine sulfhydrylase in the crystal probed by polarized absorption microspectrophotometry.
[15]
PubMed ID9914259
JournalCurr Opin Struct Biol
Year1998
Volume8
Pages759-69
AuthorsJansonius JN
TitleStructure, evolution and action of vitamin B6-dependent enzymes.
[16]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID99384139
PubMed ID10452898
JournalJ Mol Biol
Year1999
Volume291
Pages941-53
AuthorsBurkhard P, Tai CH, Ristroph CM, Cook PF, Jansonius JN
TitleLigand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium.
Related PDB1d6s
Related Swiss-protP0A1E3
[17]
PubMed ID11193402
JournalBiosci Biotechnol Biochem
Year2000
Volume64
Pages2352-9
AuthorsSugihara Y, Yamagata S, Mizuno Y, Ezaki T
TitleCharacterization of O-acetyl-L-serine sulfhydrylase purified from an alkaliphilic bacterium.
[18]
PubMed ID10995767
JournalJ Biol Chem
Year2000
Volume275
Pages40244-51
AuthorsBettati S, Benci S, Campanini B, Raboni S, Chirico G, Beretta S, Schnackerz KD, Hazlett TL, Gratton E, Mozzarelli A
TitleRole of pyridoxal 5'-phosphate in the structural stabilization of O-acetylserine sulfhydrylase.
[19]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID20481415
PubMed ID11023792
JournalJ Mol Biol
Year2000
Volume303
Pages279-86
AuthorsBurkhard P, Tai CH, Jansonius JN, Cook PF
TitleIdentification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound.
Related PDB1fcj
Related Swiss-protP0A1E3
[20]
PubMed ID10673430
JournalStructure Fold Des
Year2000
Volume8
PagesR1-6
AuthorsSchneider G, Kack H, Lindqvist Y
TitleThe manifold of vitamin B6 dependent enzymes.
[21]
PubMed ID11412097
JournalBiochemistry
Year2001
Volume40
Pages7446-52
AuthorsTai CH, Burkhard P, Gani D, Jenn T, Johnson C, Cook PF
TitleCharacterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase.
[22]
PubMed ID11259310
JournalBiophys J
Year2001
Volume80
Pages1973-85
AuthorsChirico G, Bettati S, Mozzarelli A, Chen Y, Muller JD, Gratton E
TitleMolecular heterogeneity of O-acetylserine sulfhydrylase by two-photon excited fluorescence fluctuation spectroscopy.
[23]
PubMed ID11168407
JournalEur J Biochem
Year2001
Volume268
Pages686-93
AuthorsWirtz M, Berkowitz O, Droux M, Hell R
TitleThe cysteine synthase complex from plants. Mitochondrial serine acetyltransferase from Arabidopsis thaliana carries a bifunctional domain for catalysis and protein-protein interaction.

comments
This enzyme was transferred from E.C. 4.2.99.8 to E.C. 2.5.1.47.
This enzyme belongs to the type-II PLP-dependent enzyme superfamily (or Tryptophan synthase beta-subunit family), according to the literature [15] & [20].
According to the literature [7], [8], [10], [12] & [13], this enzyme catalyzes the following reactions:
(A) Formation of external aldimine (with amine group of the first substrate, O-acetyl-serine, OAS).
(B) Isomerization (change in the position of double-bond).
(C) beta-elimination of acetyl group, forming a double-bonded beta-carbon (bound to PLP), and releasing acetate.
(D) Addition of the second substrate, sulfide, to the double-bonded beta-carbon.
(E) Isomerization (change in the position of double-bond).
(F) Formation of internal aldimine, releasing the product.

createdupdated
2004-07-152009-02-26


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 2010)
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)

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