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Information on EC 2.5.1.47 - cysteine synthase and Organism(s) Aeropyrum pernix and UniProt Accession Q9YBL2

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EC Tree
IUBMB 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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This record set is specific for:
Aeropyrum pernix
UNIPROT: Q9YBL2
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The taxonomic range for the selected organisms is: Aeropyrum pernix
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylserine sulfhydrylase
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-
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CSase
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-
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cysteine synthetase
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O-acetyl-L-serine acetate-lyase (adding hydrogen sulfide)
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O-acetyl-L-serine sulfhydrylase
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O-acetyl-L-serine sulfohydrolase
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-
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O-acetyl-L-serine(thiol)lyase
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O-acetylserine (Thiol)-lyase
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-
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O-acetylserine (thiol)lyase
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O-acetylserine sulfhydrylase
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-
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O-acetylserine sulfhydrylase A
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-
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O-acetylserine(thiol)lyase
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O-acetylserine-O-acetylhomoserine sulfhydro-lyase
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OAS Shase
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OAS-TL
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OASS
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OASTL
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S-sulfocysteine synthase
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synthase, cysteine
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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C-O bond cleavage
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-
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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 hide
37290-89-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
show the reaction diagram
-
-
-
-
?
L-homocysteine + L-serine
L-cystathionine + H2O
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
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-
?
O-acetyl-L-Ser + thiosulfate
S-sulfocysteine + sodium acetate
show the reaction diagram
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?
O-acetyl-L-serine
L-cysteine + acetate
show the reaction diagram
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?
additional information
?
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the enzyme also catalyzes the reaction of EC 2.5.1.65, O-phosphoserine hydrolase
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
crystallization data
pyridoxal 5'-phosphate
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enzyme contains 1.2 pyridoxal phosphate per subunit
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24 - 28
O-acetyl-L-Ser
21
thiosulfate
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synthesis of S-sulfo-L-cysteine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
202
H2S
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sulfhydrylation of O-acetyl-L-serine
24 - 202
O-acetyl-L-Ser
24
thiosulfate
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synthesis of S-sulfo-L-cysteine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46
pH 7.5, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
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sulfhydrylation of O-acetyl-L-serine
8.1 - 8.8
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synthesis of L-cystathionine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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maximal for O-acetyl-L-serine sulfhydrylation at both 70°C and at 80°C
80
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synthesis of L-cystathionine and sulfhydrylation of L-Ser. Maximal for O-acetyl-L-serine sulfhydrylation at both 70°C and at 80°C
90
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synthesis of S-sulfo-L-cysteine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
-
2 * 42000, SDS-PAGE
70580
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sedimentation equilibrium
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of the enzyme without acetate, the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-phosphoserine, and the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-acetylserine, to 2.1 A resolution. No significant difference is seen in the overall structure between the free and complexed forms of the enzyme. The side chains of T152, S153, and Q224 interact with the carboxylate of the substrate. The position of R297 is significantly unchanged in the complex of the K127A mutant with the external Schiff base, allowing enough space for an interaction with O-phosphoserine. The positively charged environment around the entrance of the active site including S153 and R297 is important for accepting negatively charged substrates
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K127A
mutant is inactive for cysteine synthesis and does not form the alpha-aminoacrylate intermediate
Q224A
0.2% of wild-type activity
R297A
61% of wild-type activity
R297E
52% of wild-type activity
R297K
48% of wild-type activity
S153A
117% of wild-type activity
S153T
8% of wild-type activity
T152A
2% of wild-type activity
T152S
93% of wild-type activity
T203A
41% of wild-type activity
T203M
20% of wild-type activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
pH 6.1 and 6.7, 6 h, 10% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mino, K.; Ishikawa, K.
Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1
J. Bacteriol.
185
2277-2284
2003
Aeropyrum pernix, Arabidopsis thaliana
Manually annotated by BRENDA team
Mino, K.; Oda, Y.; Ataka, M.; Ishikawa, K.
Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1
Acta Crystallogr. Sect. D
59
338-340
2003
Aeropyrum pernix
Manually annotated by BRENDA team
Nakamura, T.; Kawai, Y.; Kunimoto, K.; Iwasaki, Y.; Nishii, K.; Kataoka, M.; Ishikawa, K.
Structural analysis of the substrate recognition mechanism in O-phosphoserine sulfhydrylase from the hyperthermophilic archaeon Aeropyrum pernix K1
J. Mol. Biol.
422
33-44
2012
Aeropyrum pernix (Q9YBL2)
Manually annotated by BRENDA team