Microbial distribution of selenocysteine lyase.
We studied the distribution of selenocysteine lyase, a novel enzyme catalyzing the conversion of selenocysteine into alanine and H2Se, which we first demonstrated in various mammalian tissues (Esaki et al., J. Biol. Chem. 257:4386-4391, 1982). Enzyme activity was found in various bacteria such as Alcaligenes viscolactis and Pseudomonas alkanolytica. No significant activity was found in yeasts and fungi. Selenocysteine lyases from A. viscolactis and P. alkanolytica acted specifically on L-selenocysteine and required pyridoxal 5'-phosphate as a cofactor.
D000421:Alcaligenes / Q000201:enzymology*; D001419:Bacteria / Q000201:enzymology*; D003545:Cysteine / Q000031:analogs & derivatives / Q000378:metabolism; D003593:Cytoplasm / Q000201:enzymology; D005658:Fungi / Q000201:enzymology; D007700:Kinetics; D008190:Lyases / Q000302:isolation & purification / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D012643:Selenium / Q000378:metabolism; D017279:Selenocysteine; D015003:Yeasts / Q000201:enzymology
D017279:Selenocysteine; D011732:Pyridoxal Phosphate; D008190:Lyases; C034278:selenocysteine lyase; D012643:Selenium; D003545:Cysteine