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Purification and Characterization of S-adenosylhomocysteine Deaminase From Streptonigrin-Producing Streptomyces Flocculus

J J Zulty, M K Speedie

J Bacteriol. 1989 Dec;171(12):6840-4.

PMID: 2592350

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 degrees C, and the deaminase was inactivated by p-chloromercuribenzoate but not by metal chelators. The Km for S-adenosylhomocysteine is 2.5 mM, and the Ki for inhibition by deoxycoformycin is 1.6 nM.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP3930196 Streptonigrin from Streptomyces flocculus Streptonigrin from Streptomyces flocculus 3930-19-6 Price
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