The PatB protein of Bacillus subtilis is a C-S-lyase

Biochimie. 2005 Feb;87(2):231-8. doi: 10.1016/j.biochi.2004.09.007.

Abstract

The PatB protein of Bacillus subtilis had both cystathionine beta-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 beta-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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / enzymology*
  • Bacillus subtilis / genetics
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Carbon-Sulfur Lyases / genetics
  • Carbon-Sulfur Lyases / metabolism*
  • Cystathionine gamma-Lyase / genetics
  • Cystathionine gamma-Lyase / metabolism*
  • Cysteine Synthase / genetics
  • Cysteine Synthase / metabolism
  • Lyases / genetics
  • Lyases / metabolism*
  • Methionine / biosynthesis*
  • Methionine / genetics

Substances

  • Bacterial Proteins
  • Methionine
  • Cysteine Synthase
  • Lyases
  • Carbon-Sulfur Lyases
  • Cystathionine gamma-Lyase
  • cystathionine beta-lyase