EzCatDB: D00264
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DB codeD00264
CATH domainDomain 13.40.50.1100 : Rossmann fold
Domain 23.40.50.1100 : Rossmann foldCatalytic domain
E.C.2.5.1.47
CSA1oas

CATH domainRelated DB codes (homologues)
3.40.50.1100 : Rossmann foldT00088,T00089

Enzyme Name
UniProtKBKEGG

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
RefSeqNP_461365.1 (Protein)
NC_003197.1 (DNA/RNA sequence)
PfamPF00291 (PALP)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00272Cysteine metabolism
MAP00450Selenoamino acid metabolism
MAP00920Sulfur metabolism

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

Compound table: links to PDB-related databases & PoSSuM

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
ChEBI18405
17981
58340
16136
17561
35235
15366

PubChem1051
99478
6971051
402
18779926
6419722
5862
21980959
176

              
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 UniProtKBP0A1E3
[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 UniProtKBP0A1E3
[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 UniProtKBP0A1E3
[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
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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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