type	Journal Article
authors	Auger, S.; Gomez, M.P.; Danchin, A.; Martin-Verstraete, I.
title	The PatB protein of Bacillus subtilis is a C-S-lyase
journal	Biochimie
Activity	4.4.1.28
Family	4.4.1.28.a
sel	selected
ui	15760717
year	(2005)
volume	87
number	2
pages	231-238
keywords	Bacillus subtilis/*enzymology/genetics
abstract	he PatB protein of Bacillus subtilis had both cystathionine P-lyase and cysteine desulfhydrase activities in vitro. The apparent K-m value of the PatB protein for cystathionine was threefold higher than that of the MetC protein, the previously characterized cystathionine P-lyase of B. subtilis. In the presence of cystathionine as sole Sulfur source, the patB gene present on a multicopy plasmid restored the growth of a metC mutant. In addition. the patB metC double mutant was unable to grow in the presence of sulfate or cystine while the patB or metC single Mutants grew similarly to the wild-type strains in the presence of the same sulfur sources. In a metC mutant, the PatB protein can replace the MetC enzyme in the methionine biosynthetic pathway.
last changed	2017/09/08 10:12