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
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General Information
General Information on EC 2.5.1.65 - O-phosphoserine sulfhydrylase
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metabolism
physiological function
additional information
two biosynthetic routes to L-cysteine, each with its own specific cysteine synthase (CysK1 and CysM), are described in Mycobacterium tuberculosis, and a third putative sulfhydrylase in this pathogen, CysK2, is an S-sulfocysteine synthase, utilizing O-phosphoserine (OPS) and thiosulfate as substrates. Mycobacterial CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine, cysteine synthasis pathways overview
metabolism
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two biosynthetic routes to L-cysteine, each with its own specific cysteine synthase (CysK1 and CysM), are described in Mycobacterium tuberculosis, and a third putative sulfhydrylase in this pathogen, CysK2, is an S-sulfocysteine synthase, utilizing O-phosphoserine (OPS) and thiosulfate as substrates. Mycobacterial CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine, cysteine synthasis pathways overview
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the enzyme synthesizes S-sulfocysteine, the can also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during dormancy
physiological function
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the enzyme synthesizes S-sulfocysteine, the can also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during dormancy
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Intramolecular electrostatic interaction of enzyme OPSS, overview
additional information
three-dimensional structure analysis of enzyme ApOPSS in complex with aminoacrylate intermediate formed from pyridoxal 5'-phosphate with O-phospho-L-serine or the enzyme in complex with L-cysteine, and structure comparisons, molecular docking simulation using the structure of PDB ID 3VSA as the wild-type enzyme ApOPSS, overview
additional information
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Intramolecular electrostatic interaction of enzyme OPSS, overview
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additional information
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three-dimensional structure analysis of enzyme ApOPSS in complex with aminoacrylate intermediate formed from pyridoxal 5'-phosphate with O-phospho-L-serine or the enzyme in complex with L-cysteine, and structure comparisons, molecular docking simulation using the structure of PDB ID 3VSA as the wild-type enzyme ApOPSS, overview
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