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.
Zulty
J J
JJ
Department of Biomedicinal Chemistry, School of Pharmacy, University of Maryland, Baltimore 21201.
Speedie
M K
MK
D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008970:Molecular Weight; D009700:Nucleoside Deaminases / Q000302:isolation & purification* / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology*; D013308:Streptonigrin / Q000096:biosynthesis*
D013308:Streptonigrin; D009700:Nucleoside Deaminases; C062075:S-adenosylhomocysteine deaminase