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B6db references: 2081976

type Journal Article
authors Kamitani, H.; Esaki, N.; Tanaka, H.; Imahara, H.; Soda, K.
title Purification and characterization of S-alkylcysteine alpha,beta-lyase from Pseudomonas putida
journal J Nutr Sci Vitaminol (Tokyo)
sel selected
ui 2081976
year (1990)
volume 36
number 4
pages 339-47
keywords Amino Acids/metabolism
abstract S-Alkylcysteine alpha,beta-lyase [EC] was purified to more than 90% homogeneity from the cell extract of Pseudomonas putida ICR 3640. The enzyme has a molecular weight of about 195,000, and is composed of six subunits identical in molecular weight (37,000). Pyridoxal 5'- phosphate is required as a cofactor. The enzyme catalyzes the alpha,beta-elimination of S-methyl-L-cysteine and its analogs such as S- ethyl-L-cysteine, L-djenkolate, Se-methyl-DL-selenocysteine, and O- methyl-L-serine. However, S-methyl-D-cysteine, L-methionine, and L- norvaline were inert. The enzyme catalyzes also the beta-replacement reaction of the thiomethyl group of S-methyl-L-cysteine with various thiols to yield the corresponding S-substituted cysteines. In addition to S-methyl-L-cysteine, Se-methyl-DL-selenocysteine and O-methyl-L- serine also serve as substrates in the beta-replacement reaction.
last changed 2009/07/01 10:57

B6db references