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
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KM Value
KM Value on EC 2.5.1.65 - O-phosphoserine sulfhydrylase
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0.39
hydrogen sulfide
pH 7.5, 80°C, wild-type enzyme, with O-acetyl-L-serine
1.6
hydrogen sulfide
pH 7.5, 80°C, mutant F225A, with O-phospho-L-serine
3.8
hydrogen sulfide
pH 7.5, 80°C, wild-type enzyme, with O-phospho-L-serine
0.135
dephosphorylation, pH 7.0, 22°C, recombinant wild-type enzyme
0.485
O-phospho-L-serine
pH 7.0, 22°C, recombinant mutant R243A enzyme
1.085
O-phospho-L-serine
dephosphorylation, pH 7.0, 22°C, recombinant mutant R243A enzyme
1.086
O-phospho-L-serine
pH 7.0, 22°C, recombinant wild-type enzyme
0.044
pH 7.0, 22°C, recombinant wild-type enzyme
0.214
thiosulfate
pH 7.0, 22°C, recombinant mutant R243A enzyme
0.374
thiosulfate
dephosphorylation, pH 7.0, 22°C, recombinant wild-type enzyme
additional information
additional information
steady-state kinetics, the Km value toward O-phospho-L-serine is not significantly different between the wild-type ApOPSS and the F225A mutant, the kcat value of the wild-type ApOPSS is 4.2fold higher toward O-phospho-L-serine and 15fold higher toward O-acetyl-L-erine than that of the F225A mutant, respectively
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additional information
additional information
stopped-flow and Michaelis-Menten kinetic analysis, overview. The amino acrylate reaction intermediate is not stable and decomposes with a pseudo-first-order rate constant kobs of 0.12/s
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additional information
additional information
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stopped-flow and Michaelis-Menten kinetic analysis, overview. The amino acrylate reaction intermediate is not stable and decomposes with a pseudo-first-order rate constant kobs of 0.12/s
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