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Literature summary extracted from

  • Mino, K.; Ishikawa, K.
    A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1 (2003), FEBS Lett., 551, 133-138.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.5.1.65 dithiothreitol slightly activates the O-phospho-L-serine sulfhydrylation reaction Aeropyrum pernix

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.65 expression in Escherichia coli Rosetta (DE3) Aeropyrum pernix

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.65 3-chloro-D-alanine 18% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 3-Cyano-L-alanine 42% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 Cd2+ slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation Aeropyrum pernix
2.5.1.65 CdCl2 25°C, 10 min, 26% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 15% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 Co2+ strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation Aeropyrum pernix
2.5.1.65 CoCl2 25°C, 10 min, 61% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 98.8% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 Cu2+ strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation Aeropyrum pernix
2.5.1.65 CuCl2 25°C, 10 min, 79% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 98.7% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 Fe2+ slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation Aeropyrum pernix
2.5.1.65 Fe3+ strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation Aeropyrum pernix
2.5.1.65 FeCl2 25°C, 10 min, 20% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 27% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 FeCl3 25°C, 10 min, 25% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 96.1% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 Hg2+ strongly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation Aeropyrum pernix
2.5.1.65 HgCl2 25°C, 10 min, 98.3% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 80% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 additional information no inhibition by O-phospho-D-serine, EDTA, 2-mercaptoethanol, DTT, NEM, PCMB, and Gd3+, while Ca2+, K+, Na+, Mn2+, and Mg2+ are poor inhibitors; no inhibition of the O-acetyl-L-serine sulfhydrylation reaction by O-phospho-D-serine Aeropyrum pernix
2.5.1.65 Ni2+ strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation Aeropyrum pernix
2.5.1.65 NiCl2 25°C, 10 min, 15% inhibition of the O-phospho-L-serine sulfhydrylation reaction, almost complete inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 O-benzyl-L-serine 36% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 O-tert-butyl-L-serine 49% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 Pb(CH3COO)2 25°C, 10 min, 95% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 88% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 Pb2+ strongly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation Aeropyrum pernix
2.5.1.65 Zn2+ slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation Aeropyrum pernix
2.5.1.65 ZnCl2 25°C, 10 min, 23% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 25% inhibition of the O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.65 additional information
-
additional information kinetics Aeropyrum pernix
2.5.1.65 additional information
-
additional information ping-pong bi-bi mechanism Aeropyrum pernix
2.5.1.65 0.25
-
Sulfide 60°C, O-acetyl-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 0.25
-
hydrogen sulfide pH 7.6, 60°C, with O-acetyl-L-serine Aeropyrum pernix
2.5.1.65 5
-
Sulfide 60°C, O-phospho-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 5
-
hydrogen sulfide pH 7.6, 60°C, with O-phospho-L-serine Aeropyrum pernix
2.5.1.65 12.5
-
Sulfide 85°C, O-phospho-L-serine sulfhydrylation reaction Aeropyrum pernix
2.5.1.65 12.5
-
hydrogen sulfide pH 7.6, 85°C, with O-phospho-L-serine Aeropyrum pernix
2.5.1.65 21
-
O-acetyl-L-serine 60°C Aeropyrum pernix
2.5.1.65 21
-
O-acetyl-L-serine pH 7.6, 60°C Aeropyrum pernix
2.5.1.65 200
-
O-phospho-L-serine 60°C Aeropyrum pernix
2.5.1.65 200
-
O-phospho-L-serine pH 7.6, 60°C Aeropyrum pernix
2.5.1.65 250
-
O-phospho-L-serine 85°C Aeropyrum pernix
2.5.1.65 250
-
O-phospho-L-serine pH 7.6, 85°C Aeropyrum pernix

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.65 42000
-
2 * 42000 Aeropyrum pernix

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.65 additional information Aeropyrum pernix L-cysteine biosynthesis ?
-
?
2.5.1.65 O-acetyl-L-serine + hydrogen sulfide Aeropyrum pernix enzyme is involved in L-cysteine biosynthesis, pathway overview L-cysteine + acetate
-
ir
2.5.1.65 O-phospho-L-serine + hydrogen sulfide Aeropyrum pernix enzyme is involved in L-cysteine biosynthesis, pathway overview L-cysteine + phosphate
-
ir

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.65 Aeropyrum pernix
-
-
-
2.5.1.65 Aeropyrum pernix
-
hyperthermophilic archeon
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.65 recombinant OASS Aeropyrum pernix

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.65 O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate ping-pong bi-bi mechanism Aeropyrum pernix

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.65 54.5
-
60°C, O-acetyl-L-serine sulfhydrylation reaction, recombinant OASS Aeropyrum pernix

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.65 3-chloro-L-alanine + hydrogen sulfide
-
Aeropyrum pernix ?
-
ir
2.5.1.65 3-chloro-L-alanine + sulfide heat-labile substrate, 173% of activity compared with O-acetyl-L-serine as substrate Aeropyrum pernix ?
-
?
2.5.1.65 L-azaserine + hydrogen sulfide O-phospho-L-serine is a heat-stable substrate Aeropyrum pernix ?
-
ir
2.5.1.65 L-azaserine + sulfide same activity as with O-acetyl-L-serine as substrate Aeropyrum pernix ?
-
?
2.5.1.65 additional information L-cysteine biosynthesis Aeropyrum pernix ?
-
?
2.5.1.65 additional information 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 Aeropyrum pernix ?
-
?
2.5.1.65 additional information 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 Aeropyrum pernix ?
-
?
2.5.1.65 O-acetyl-L-serine + hydrogen sulfide enzyme is involved in L-cysteine biosynthesis, pathway overview Aeropyrum pernix L-cysteine + acetate
-
ir
2.5.1.65 O-acetyl-L-serine + hydrogen sulfide O-acetyl-L-serine is a heat-labile substrate Aeropyrum pernix L-cysteine + acetate
-
ir
2.5.1.65 O-acetyl-L-serine + sulfide heat-labile substrate Aeropyrum pernix L-cysteine + acetic acid
-
?
2.5.1.65 O-phospho-L-serine + hydrogen sulfide enzyme is involved in L-cysteine biosynthesis, pathway overview Aeropyrum pernix L-cysteine + phosphate
-
ir
2.5.1.65 O-phospho-L-serine + hydrogen sulfide O-phospho-L-serine is a heat-stable substrate Aeropyrum pernix L-cysteine + phosphate
-
ir
2.5.1.65 O-phospho-L-serine + sulfide 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 Aeropyrum pernix L-cysteine + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
2.5.1.65 dimer 2 * 42000 Aeropyrum pernix

Synonyms

EC Number Synonyms Comment Organism
2.5.1.65 O-acetylserine sulfhydrylase
-
Aeropyrum pernix
2.5.1.65 OASS
-
Aeropyrum pernix

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.65 70
-
sulfhydrylation of 3-chloro-L-alanine Aeropyrum pernix
2.5.1.65 70
-
with substrate 3-chloro-L-alanine Aeropyrum pernix
2.5.1.65 80
-
sulfhydrylation of L-azaserine Aeropyrum pernix
2.5.1.65 80
-
with substrate L-azaserine Aeropyrum pernix
2.5.1.65 90
-
sulfhydrylation of O-phospho-L-serine Aeropyrum pernix
2.5.1.65 90
-
with substrate O-phospho-L-serine Aeropyrum pernix

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.5.1.65 90
-
50% of maximum activity with 3-chloro-L-alanine as substrate Aeropyrum pernix

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.65 156
-
O-acetyl-L-serine 60°C Aeropyrum pernix
2.5.1.65 156
-
O-acetyl-L-serine pH 7.6, 60°C Aeropyrum pernix
2.5.1.65 3050
-
O-phospho-L-serine 60°C Aeropyrum pernix
2.5.1.65 3050
-
O-phospho-L-serine pH 7.6, 60°C Aeropyrum pernix
2.5.1.65 14000
-
O-phospho-L-serine 85°C Aeropyrum pernix
2.5.1.65 14000
-
O-phospho-L-serine pH 7.6, 85°C Aeropyrum pernix

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.65 7.3 8.1 at 85°C Aeropyrum pernix
2.5.1.65 7.3 8.1 dependent on the substrate, overview Aeropyrum pernix

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.65 pyridoxal 5'-phosphate dependent on Aeropyrum pernix
2.5.1.65 pyridoxal 5'-phosphate pyridoxal 5'-phosphate-dependent Aeropyrum pernix