Purification and characterization of S-adenosylhomocysteine deaminase from streptonigrin-producing Streptomyces flocculus

J. J. Zulty, M. K. Speedie

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9 Scopus citations

Abstract

An S-adenosylhomocysteine deaminase has been isolated and purified from streptonigrin-producing Streptomyces flocculus ATCC 13257. Deamination represents the major metabolic route of S-adenosylhomocysteine in this organism. The protein was found to be monomeric with a molecular weight of 56,100 ± 1,600. The activity was optimal at pH 7.0 and 37°C, and the deaminase was inactivated by p-chloromercuribenzoate but not by metal chelators. The K(m) for S-adenosylhomocysteine is 2.5 mM, and the K(i) for inhibition by deoxycoformycin is 1.6 nM.

Original languageEnglish (US)
Pages (from-to)6840-6844
Number of pages5
JournalJournal of bacteriology
Volume171
Issue number12
DOIs
StatePublished - 1989

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