1887

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.

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2002-12-01
2020-09-29
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