Enzymes of Neisseria gonorrhoeae and Other Neisseria

Tauber, Henry; Russell, Harold

doi:10.3181/00379727-110-27543

Cited by 8 publications

(3 citation statements)

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“…When cell-free extracts were fractionated into membranous and supernatant fractions, nearly all activity was associated with the membranous fraction of the cell. In contrast to the L-amino acid oxidases reported in other bacteria (5,28), the one in meningococcal membranes exhibited a relatively limited specificity. Of the amino acids tested, only L-cysteine, D-cysteine, and cysteamine produced detectable oxygen consumption ( Table 2).…”

Section: Resultscontrasting

confidence: 71%

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L-cysteine oxidase activity in the membrane of Neisseria meningitidis

Yu¹,

DeVoe²

1981

J Bacteriol

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Among the L-amino acids, only L-cysteine was oxidized by isolated washed membranes of group B Neisseria meningitidis SD1C. The cysteine oxidase in the membrane obeyed Michaelis-Menten kinetics and was heat labile. The pH optimum for the maximum velocity of the reaction was 9.8. Specific activity of the enzyme increased as cell growth progressed through the exponential phase toward the stationary phase of growth. The enzyme activity was markedly sensitive to inhibition by metal chelators, but was resistant to inhibitors of terminal oxidases with the exception of cyanide. All known cytochromes in the membrane, except b56, were reduced with L-cysteine. The additive nature of Lcysteine oxidase and succinate oxidase activities suggests that an unidentified oxidase is involved in the oxidation of cysteine.

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Section: Resultscontrasting

confidence: 71%

“…In an earlier report on the cysteine oxidase of Neisseria, Tauber and Russell (28) concluded that the product of the cysteine-oxidase reaction v X was cystine. layer chromatography, amino acid analysis, or ference spectrum (250C) of the envelope preparation column separation ofthe reaction products (data of the meningococcus.…”

Section: 7mentioning

confidence: 99%