1887

Microbiology

Volume 148, Issue 12

from encodes a C-S lyase with α,β-elimination activity that degrades -cysteine Free

Abstract

Hydrogen sulfide is highly toxic to mammalian cells. It has also been postulated that hydrogen sulfide modifies haemoglobin resulting in haemolysis. The enzyme that produces hydrogen sulfide from L-cysteine was purified from . Using the N-terminal amino acid sequence of the purified enzyme, the gene encoding L-cysteine desulfhydrase was cloned; the recombinant protein was then purified to examine its enzymic and biological characteristics. This L-cysteine desulfhydrase had the Michaelis–Menten kinetics =062 mM and =163 μmol min mg. DL-Cystathionine, L-cystine, -(2-aminoethyl)-L-cysteine, 3-chloro-DL-alanine and -methyl-L-cysteine were substrates for the enzyme, whereas D-cysteine, DL-homocysteine, L-methionine, DL-serine, DL-alanine, L-cysteine methyl ester, L-tryptophan, L-tyrosine and L-phenylalanine were not. These findings suggest that this L-cysteine desulfhydrase is a C-S lyase that catalyses the α,β-elimination (αC-N and βC-S) reaction. In addition, it is demonstrated that the hydrogen sulfide produced by this enzyme caused the modification and release of haemoglobin in sheep erythrocytes.

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): hydrogen sulfide , l-cysteine desulfhydrase and RBC, sheep erythrocyte
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2002-12-01
2019-11-20
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lcd from Streptococcus anginosus encodes a C-S lyase with α,β-elimination activity that degrades l-cysteine
Microbiology 148, 3961 (2002); https://doi.org/10.1099/00221287-148-12-3961
/content/journal/micro/10.1099/00221287-148-12-3961
/content/journal/micro/10.1099/00221287-148-12-3961
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