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Information on EC 2.5.1.47 - cysteine synthase and Organism(s) Streptomyces lavendulae and UniProt Accession D2Z027
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2.5.1.47 cysteine synthaseIUBMB Comments
A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (beta-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
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Word Map
- 2.5.1.47
- h2s
- sulfur
- l-cysteine
- gsh
-
gamma-glutamyl
- acetyltransferase
- pyridoxal
-
slow-releasing
- typhimurium
- 5'-phosphate
-
gasotransmitter
-
o-acetylserinethiollyase
- nahs
- sulfite
-
gaseous
-
schiff
-
buthionine
- sulfoximine
- phytochelatins
-
assimilatory
-
plp-dependent
- desulfhydrase
-
h2s-releasing
- alpha-aminoacrylate
- thiosulfate
- oxygenase-1
- gamma-gcs
- sulphide
- dl-propargylglycine
-
transsulfuration
-
bienzyme
- 3-mercaptopyruvate
-
5'-phosphate-dependent
- beta-synthase
-
h2s-producing
-
sulfurylase
-
aldimine
-
beta-replacement
-
gamma-lyase
- sulfurtransferase
- cysb
- hydrosulfide
- biotechnology
- agriculture
- synthesis
- pharmacology
- medicine
- environmental protection
- drug development
- analysis
The taxonomic range for the selected organisms is: Streptomyces lavendulae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
gyy4137, cysteine synthase, cysteine synthetase, o-acetylserine sulfhydrylase, oastl, oas-tl, o-acetylserine(thiol)lyase, csase, o-acetylserine (thiol) lyase, oass-a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylserine sulfhydrylase
-
-
-
-
CSase
-
-
-
-
cysteine synthetase
-
-
-
-
O-acetyl-L-serine acetate-lyase (adding hydrogen sulfide)
-
-
-
-
O-acetyl-L-serine sulfhydrylase
-
-
-
-
O-acetyl-L-serine sulfohydrolase
-
-
-
-
O-acetyl-L-serine(thiol)lyase
-
-
-
-
O-acetylserine (Thiol)-lyase
-
-
-
-
O-acetylserine (thiol)lyase
-
-
-
-
O-acetylserine sulfhydrylase
-
-
-
-
O-acetylserine sulfhydrylase A
-
-
-
-
O-acetylserine(thiol)lyase
-
-
-
-
O-acetylserine-O-acetylhomoserine sulfhydro-lyase
-
-
-
-
OAS Shase
-
-
-
-
OAS-TL
-
-
-
-
OASS
-
-
-
-
OASTL
-
-
-
-
S-sulfocysteine synthase
-
-
-
-
synthase, cysteine
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
C-O bond cleavage
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (beta-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
CAS REGISTRY NUMBER
COMMENTARY
37290-89-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme catalyzes the reaction with O-acetyl-L-serine and hydroxyurea with 80fold lower catalytic efficiency
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
additional information
?
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
?
additional information
?
-
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
O-acetyl-L-serine
30°C, pH 8.0, cosubstrate: hydrogen sulfide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
both in solution and in a crystalline state, crystallization data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant K43A, to 2.25 and 1.9 A resolution, respectively. Each monomer of DcsD takes a typical fold of type II pyridoxal 5'-phosphate enzymes with the cofactor pyridoxal 5'-phosphate covalently bound to invariant Lys residue (Lys43) at the active site. The pyridine ring of pyridoxal 5'-phoshate makes hydrogen bonds with invariant Asn73 and Ser265 residues. Its phosphate group makes hydrogen bonds with Gly177, Thr178, Thr179 and Thr181 residues
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K43A
mutation in invariant Lys43 residue, inactive. Mutant forms an external aldimine adduct upon addition of L-methionine or O-ureido-L-serine
S121A
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
S121M
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
V74T
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
Y97F
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
Y97M
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Uda, N.; Matoba, Y.; Kumagai, T.; Oda, K.; Noda, M.; Sugiyama, M
. Establishment of an in vitro D-cycloserine-synthesizing system by using O-ureido-L-serine synthase and D-cycloserine synthetase found in the biosynthetic pathway
Antimicrob. Agents Chemother.
57
2603-2612
2013
Streptomyces lavendulae (D2Z027), Streptomyces lavendulae ATCC 11924 (D2Z027)
Uda, N.; Matoba, Y.; Oda, K.; Kumagai, T.; Sugiyama, M.
The structural and mutational analyses of O-ureido-L-serine synthase necessary for D-cycloserine biosynthesis
FEBS J.
282
3929-3944
2015
Streptomyces lavendulae (D2Z027), Streptomyces lavendulae, Streptomyces lavendulae ATCC 11924 (D2Z027)
EXTERNAL LINKS (specific for EC-Number 2.5.1.47)
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Release 2023.1 (January 2023)
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