Journal Article

Cystalysin, a 46-kDa <span class="smallCaps">L</span>-Cysteine Desulfhydrase from <i>Treponema denticola</i>: Biochemical and Biophysical Characterization

Lianrui Chu, Jeffery L. Ebersole, Gary P. Kurzban and Stanley C. Holt

in Clinical Infectious Diseases

Published on behalf of Infectious Diseases Society of America

Volume 28, issue 3, pages 442-450
Published in print March 1999 | ISSN: 1058-4838
Published online March 1999 | e-ISSN: 1537-6591 | DOI: http://dx.doi.org/10.1086/515164
Cystalysin, a 46-kDa L-Cysteine Desulfhydrase from Treponema denticola: Biochemical and Biophysical Characterization

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A 46-kDa hemolytic protein referred to as cystalysin, from Treponema denticola ATCC 35404, was characterized and overexpressed in Escherichia coli LC-67. Cystalysin lysed erythrocytes, hemoxidized hemoglobin to sulfhemoglobin and methemoglobin, and removed the sulfhydryl and amino group from selected S-containing compounds (e.g., cysteine) producing H2S, NH3, and pyruvate. With L-cysteine as substrate, cystalysin obeys Michaelis-Menten kinetics. Cystathionine and s-aminoethyl-L-cysteine were also substrates. Several of the small alpha amino acids were found to be competitive inhibitors of cystalysin. The enzymatic activity was increased by β-mercaptoethanol and was not inhibited by the proteinase inhibitor TLCK (Nα-p-tosyl-L-lysine chloromethyl ketone), pronase, or proteinase K, suggesting the functional site was physically protected or located in a small fragment of the polypeptide. We hypothesize that cystalysin is a pyridoxal-5-phosphatecontaining enzyme with the activity of an αC-N and βC-S lyase (cystathionase). Since high amounts of H2S have been reported in deep periodontal pockets, this metabolic enzyme from T. denticola may also function in vivo as an important virulence molecule.

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Subjects: Infectious Diseases ; Immunology ; Public Health and Epidemiology ; Microbiology

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