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2.8.5.1 |
Description |
S-sulfo-L-cysteine synthase (3-phospho-L-serine-dependent) |
Alternative names |
cysK2 (gene name) |
Catalyzed reaction |
O-phospho-L-serine + thiosulfate = S-sulfo-L-cysteine + phosphate |
Cofactor |
Pyridoxal phosphate |
Comments |
The enzyme, which has been characterized from the bacterium Mycobacterium tuberculosis, has no activity with O-acetyl-L-serine. Requires pyridoxal 5'-phosphate. cf. EC 2.5.1.144, S-sulfo-L-cysteine synthase (O-acetyl-L-serine-dependent). |
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Mycobacterial CysK2 provides an alternative metabolic rout to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. Mycobacterium tubercolosis infects macrophages evading the bacterial action of immune cells. S-sulfocysteine could also acts as a signaling molecule triggering additional responses in redox defense upon exposure to reactive oxygen species. |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 2.8.5.1
BRENDA (activities) 2.8.5.1
KEGG (pathways) 2.8.5.1
PLPMDB (PLP mutants) 2.8.5.1
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References |
Articles on 2.8.5.1 |
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last changed |
2018/06/04 11:54 |
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