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 language | English (US) |
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Pages (from-to) | 6840-6844 |
Number of pages | 5 |
Journal | Journal of bacteriology |
Volume | 171 |
Issue number | 12 |
DOIs | |
State | Published - 1989 |