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

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Zulty JJ,Speedie MK

doi

10.1128/jb.171.12.6840-6844.1989

subject

Has Abstract

pub_date

1989-12-01 00:00:00

pages

6840-4

issue

12

eissn

0021-9193

issn

1098-5530

journal_volume

171

pub_type

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