2.5.1.65: O-phosphoserine sulfhydrylase
This is an abbreviated version!
For detailed information about O-phosphoserine sulfhydrylase, go to the full flat file.
Word Map on EC 2.5.1.65
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2.5.1.65
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oropharyngeal
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aeropyrum
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pernix
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o-acetyl-l-serine
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o-acetylserine
- 2.5.1.65
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oropharyngeal
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aeropyrum
- pernix
- o-acetyl-l-serine
- o-acetylserine
Reaction
Synonyms
APE1586, ApOPSS, CysK2, CysM, O-acetyl-L-serine sulfhydrylase, O-acetylserine sulfhydrylase, O-phospho-L-serine sulfhydrylase, O-phospho-L-serine-dependent S-sulfocysteine synthase, O-phosphoserine S-sulfocysteine synthase, O-phosphoserine specific cysteine synthase, O-phosphoserine(thiol)-lyase, OASS, OPSS, Rv1336, S-sulfocysteine synthase
ECTree
2.5.1.65 O-phosphoserine sulfhydrylaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.5.1.65 - O-phosphoserine sulfhydrylase
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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
3-chloro-L-alanine + sulfide
?
-
heat-labile substrate, 173% of activity compared with O-acetyl-L-serine as substrate
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-
?
L-azaserine + hydrogen sulfide
?
-
O-phospho-L-serine is a heat-stable substrate
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-
ir
L-azaserine + sulfide
?
-
same activity as with O-acetyl-L-serine as substrate
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + sulfide
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OASS has a high activity in the L-cysteine desulfurization reaction
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-
?
O-phospho-L-serine + sulfide
L-cysteine + phosphate
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heat-stabile substrate, 219% of activity compared with O-acetyl-L-serine as substrate, best substrate at pH 6.7 and 60°C, formation of an alpha-aminoacrylate intermediate between O-phospho-L-serine and pyridoxal 5-phosphate
-
-
?
O3-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
low activity
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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enzyme is involved in L-cysteine biosynthesis, pathway overview
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ir
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine is a heat-labile substrate
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ir
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
low activity
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + sulfide
L-cysteine + acetic acid
-
heat-labile substrate
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
best substrate
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
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enzyme is involved in L-cysteine biosynthesis
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-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
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enzyme is involved in L-cysteine biosynthesis, pathway overview
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ir
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
O-phospho-L-serine is a heat-stable substrate
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ir
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
residue Arg297 near the entrance of the active site and is important for O-phospho-L-serine substrate recognition
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-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
residue Arg297 near the entrance of the active site and is important for O-phospho-L-serine substrate recognition
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
best substrate
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
-
-
-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
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-
-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
CysK2 utilizes O-phospho-L-serine and thiosulfate as acceptor and preferred sulfur donor substrates in a pyridoxal 5'-phosphate-dependent reaction resulting in the formation of S-sulfocysteine
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-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
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-
-
?
O-phospho-L-serine + thiosulfate
S-sulfocysteine + phosphate
CysK2 utilizes O-phospho-L-serine and thiosulfate as acceptor and preferred sulfur donor substrates in a pyridoxal 5'-phosphate-dependent reaction resulting in the formation of S-sulfocysteine
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?
additional information
?
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enzyme with cystathionine beta-synthase and O-acetylserine sulfhydrylase activity in vitro, OASS has also L-serine sulfhydrylation and S-sulfo-L-cysteine synthesis activity
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?
additional information
?
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not: 3-chloro-D-alanine, 3-cyano-L-alanine, O-benzyl-L-serine, O-tert-butyl-L-serine, O-phospho-D-serine, O-succinyl-L-homoserine, L-homoserine
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?
additional information
?
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substrate specificity, no activity with 3-chloro-D-alanine, 3-cyano-L-alanine, O-benzyl-L-serine, O-tert-butyl-L-serine, O-phospho-D-serine, O-succinyl-L-homoserine, and L-homoserine
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-
?
additional information
?
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the enzyme also shows low L-cystathionine forming activity
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-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.5.1.47, cysteine synthase
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-
?
additional information
?
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OPSS is able to catalyze the synthetic reactions of various unnatural amino acids from OPS and nucleophiles that can substitute for sulfide
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?
additional information
?
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the enzyme is also active with O-acetyl-L-serine, cf. EC 2.5.1.47. When other nucleophiles are used instead of sulfide, enzyme ApOPSS produces the corresponding non-natural amino acid, when thiosulfate is used as nucleophile, for example, S-sulfocysteine is produced. In absence of sulfide, the primary substrate reacts with to pyridoxal 5'-phosphate in enzyme OPSS to yield an alpha-aminoacrylate intermediate, which is formed through an external Schiff base with the elimination of phosphate or acetate, the intermediate is finally degraded to pyruvate and pyridoxal 5'-phosphate by a water molecule without a nucleophile
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?
additional information
?
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OPSS is able to catalyze the synthetic reactions of various unnatural amino acids from OPS and nucleophiles that can substitute for sulfide
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?
additional information
?
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the enzyme is also active with O-acetyl-L-serine, cf. EC 2.5.1.47. When other nucleophiles are used instead of sulfide, enzyme ApOPSS produces the corresponding non-natural amino acid, when thiosulfate is used as nucleophile, for example, S-sulfocysteine is produced. In absence of sulfide, the primary substrate reacts with to pyridoxal 5'-phosphate in enzyme OPSS to yield an alpha-aminoacrylate intermediate, which is formed through an external Schiff base with the elimination of phosphate or acetate, the intermediate is finally degraded to pyruvate and pyridoxal 5'-phosphate by a water molecule without a nucleophile
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?
additional information
?
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enzyme is involved in an O-phosphoserine based cysteine biosynthesis pathway in Mycobacterium tuberculosis that is independent of both O-acetylserine and the sulphate reduction pathway
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?
additional information
?
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enzyme is involved in an O-phosphoserine based cysteine biosynthesis pathway in Mycobacterium tuberculosis that is independent of both O-acetylserine and the sulphate reduction pathway
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?
additional information
?
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O-acetylserine is not a substrate. Enzyme does not catalyze the reaction of EC 2.5.1.47, O-acetylserine sulfhydrolases
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?
additional information
?
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O-acetylserine is not a substrate. Enzyme does not catalyze the reaction of EC 2.5.1.47, O-acetylserine sulfhydrolases
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?
additional information
?
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specificity of CysM for its amino acid substrate is more than 500-fold greater for O-phospho-L-serine than for O-acetyl-L-serine. Specificity of CysM for this physiological sulfide equivalent, sulfur carrier protein CysO-COSH, is more than 3 orders of magnitude greater than that for bisulfide. CysM active site with the bound aminoacrylate intermediate is protected from solvent and that binding of CysO-COSH produces a conformational change allowing rapid sulfur transfer
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?
additional information
?
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the enzyme uses a mechanism via a central aminoacrylate intermediate that is similar to that of other members of this pyridoxal 5'-phosphate-dependent enzyme family. Enzyme CysK2 does not utilize thiocarboxylated CysO as a sulfur donor but accepts thiosulfate and sulfide as donor substrates, the specificity constant kcat/Km of CysK2 for thiosulfate is 40fold higher than for sulfide, suggesting an annotation as S-sulfocysteine synthase. No significant activity with O-acetyl-L-serine, Asp, Val, Gln, Glu, Ser, Asn, Cys, Ser, Leu, homocysteine, ketoacids such as pyruvate and 2-oxoglutarate, amino acid precursors like 3-phosphoglycerate and succinate, and derivatives like N-acetylcysteine and diaminopimelic acid
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-
?
additional information
?
-
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the enzyme uses a mechanism via a central aminoacrylate intermediate that is similar to that of other members of this pyridoxal 5'-phosphate-dependent enzyme family. Enzyme CysK2 does not utilize thiocarboxylated CysO as a sulfur donor but accepts thiosulfate and sulfide as donor substrates, the specificity constant kcat/Km of CysK2 for thiosulfate is 40fold higher than for sulfide, suggesting an annotation as S-sulfocysteine synthase. No significant activity with O-acetyl-L-serine, Asp, Val, Gln, Glu, Ser, Asn, Cys, Ser, Leu, homocysteine, ketoacids such as pyruvate and 2-oxoglutarate, amino acid precursors like 3-phosphoglycerate and succinate, and derivatives like N-acetylcysteine and diaminopimelic acid
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-
?
additional information
?
-
enzyme is involved in an O-phosphoserine based cysteine biosynthesis pathway in Mycobacterium tuberculosis that is independent of both O-acetylserine and the sulphate reduction pathway
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-
?
additional information
?
-
O-acetylserine is not a substrate. Enzyme does not catalyze the reaction of EC 2.5.1.47, O-acetylserine sulfhydrolases
-
-
?
additional information
?
-
the enzyme uses a mechanism via a central aminoacrylate intermediate that is similar to that of other members of this pyridoxal 5'-phosphate-dependent enzyme family. Enzyme CysK2 does not utilize thiocarboxylated CysO as a sulfur donor but accepts thiosulfate and sulfide as donor substrates, the specificity constant kcat/Km of CysK2 for thiosulfate is 40fold higher than for sulfide, suggesting an annotation as S-sulfocysteine synthase. No significant activity with O-acetyl-L-serine, Asp, Val, Gln, Glu, Ser, Asn, Cys, Ser, Leu, homocysteine, ketoacids such as pyruvate and 2-oxoglutarate, amino acid precursors like 3-phosphoglycerate and succinate, and derivatives like N-acetylcysteine and diaminopimelic acid
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?
