Differences in the betaC-S lyase activities of viridans group streptococci.

Abstract:

:betaC-S Lyase catalyzes the alpha,beta-elimination of L-cysteine to hydrogen sulfide, which is one of the main causes of oral malodor and is highly toxic to mammalian cells. We evaluated the capacity of six species of oral streptococci to produce hydrogen sulfide. The crude enzyme extract from Streptococcus anginosus had the greatest capacity. However, comparative analysis of amino acid sequences did not detect any meaningful differences in the S. anginosus betaC-S lyase. The capacity of S. anginosus purified betaC-S lyase to degrade L-cysteine was also extremely high, while its capacity to degrade L-cystathionine was unremarkable. These findings suggest that the extremely high capacity of S. anginosus to produce hydrogen sulfide is due to the unique characteristic of betaC-S lyase from that organism.

authors

Yoshida Y,Negishi M,Amano A,Oho T,Nakano Y

doi

10.1016/s0006-291x(02)02803-6

subject

Has Abstract

pub_date

2003-01-03 00:00:00

pages

55-60

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X02028036

journal_volume

300

pub_type

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