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aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
PatB family C-S lyase
Characterized members of this subfamily are known or probable C-S lyases from a family of pyridoxal phosphate-dependent enzymes that tend to be (mis)annotated as probable aminotransferases. One member is PatB of Bacillus subtilis, a proven C-S-lyase. Another is the virulence factor cystalysin from Treponema denticola, whose hemolysin activity may stem from H2S production. Members of the seed alignment occur next to examples of the enzyme 5-histidylcysteine sulfoxide synthase, from ovothiol A biosynthesis, and would be expected to perform a C-S cleavage of 5-histidylcysteine sulfoxide to leave 1-methyl-4-mercaptohistidine (ovothiol A). The PatB from Staphylococcus hominis (ShPatB) is a C-S lyase active on aliphatic cysteine-S-conjugates; its release of the thioalcohol 3-methyl-3-sulfanylhexan-1-ol (3M3SH) from the odourless precursor Cys-Gly-3M3SH secreted from human skin is a major contributor to body odor.
MalY/PatB family protein
MalY/PatB family protein acts as a beta-cystathionase, catalyzing the transformation of cystathionine to homocysteine, similar to Escherichia coli MalY and Bacillus subtilis PatB; belongs to the pyridoxal phosphate (PLP)-dependent aminotransferase superfamily
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