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Research Paper |
,ß-elimination activity that degrades L-cysteine
Department of Preventive Dentistry, Kyushu University Faculty of Dental Science, Fukuoka 812-8582, Japan1
Author for correspondence: Yoshio Nakano. Tel: +81 92 642 6423. Fax: +81 92 642 6354. e-mail: yosh{at}dent.kyushu-u.ac.jp
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 Streptococcus anginosus. Using the N-terminal amino acid sequence of the purified enzyme, the lcd 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 Km=0·62 mM and Vmax=163 µmol min-1 mg-1. DL-Cystathionine, L-cystine, S-(2-aminoethyl)-L-cysteine, 3-chloro-DL-alanine and S-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 
,ß-elimination (C-N and ßC-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.
Keywords: L-cysteine desulfhydrase, hydrogen sulfide
Abbreviations: RBC, sheep erythrocyte
The DDBJ accession number for the Streptococcus anginosus lcd gene sequence reported in this paper is AB084812.
a 
Deceased, October 14, 2001. This paper is in recognition of his fine work and is dedicated to his memory.
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