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Properties of Recombinant Staphylococcus haemolyticus Cystathionine β ‐Lyase ( metC ) and Its Potential Role in the Generation of Volatile Thiols in Axillary Malodor
Author(s) -
Troccaz Myriam,
Benattia Faiza,
Borchard Gerrit,
Clark Anthony J.
Publication year - 2008
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.200890202
Subject(s) - chemistry , recombinant dna , cystathionine beta synthase , lyase , biochemistry , staphylococcus haemolyticus , stereochemistry , enzyme , staphylococcus aureus , combinatorial chemistry , cysteine , staphylococcus , bacteria , genetics , gene , biology
Enzymes implicated in cysteine and methionine metabolism such as cystathionine β ‐lyase (CBL; EC 4.4.1.8), a pyridoxal‐5′‐phosphate (PLP)‐dependent carbon–sulfur lyase, have been shown to play a central role in the generation of sulfur compounds. This work describes the unprecedented cloning and characterization of the metC ‐cystathionine β ‐lyase from the axillary‐isolated strain Staphylococcus haemolyticus AX3, in order to determine its activity and its involvement in amino acid biosynthesis, and in the generation of sulfur compounds in human sweat. The gene contains a cysteine/methionine metabolism enzyme pattern, and also a sequence capable to effect β ‐elimination. The recombinant enzyme was shown to cleave cystathionine into homocysteine and to convert methionine into methanethiol at low levels. No odor was generated after incubation of the recombinant enzyme with sterile human axillary secretions; sweat components were found to have an inhibitory effect. These results suggest that the generation of sulfur compounds by Staphylococci and the β ‐lyase activity in human sweat are mediated by enzymes other than the metC gene or by the concerted activities of more than one enzyme.