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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Purification and characterization of S-adenosylhomocysteine deaminase from streptonigrin-producing Streptomyces flocculus. Zulty, J.J., Speedie, M.K. J. Bacteriol. (1989) [Pubmed]
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