Activation of lysine 2,3-aminomutase by S-adenosylmethionine.
نویسندگان
چکیده
منابع مشابه
S-adenosylmethionine: a 'poor man's coenzyme B12' in the reaction of lysine 2,3-aminomutase.
S-Adenosylmethionine (SAM) and an iron-sulphur centre function in place of adenosylcobalamin. Because of its coenzyme BJike role in this reaction, SAM was originally described by H. A. Barker as ‘A poor man’s adenosylcobalamin’ [4]. The conversion of lysine into P-lysine by lysine 2,3-aminomutase proceeds without exchange of solvent protons with substrate hydrogen, and by the stereochemistry il...
متن کاملMetal cofactors of lysine-2,3-aminomutase.
Lysine-2,3-aminomutase from Clostridium SB4 contains iron and sulfide in equimolar amounts, as well as cobalt, zinc, and copper. The iron and sulfide apparently constitute an Fe-S cluster that is required as a cofactor of the enzyme. Although no B12 derivative can be detected, enzyme-bound cobalt is a cofactor; however, the zinc and copper bound to the enzyme do not appear to play a role in its...
متن کاملMechanistic and Spectroscopic Studies of Lysine 2,3-Aminomutase
Lysine 2,3-aminomutase (LAM) catalyzes the interconversion of L-lysine to L-β-lysine using a [4Fe4S] cluster, S-adenosyl-L-methionine (SAM), and pyridoxal 5’-phosphate (PLP). LAM is a member of the radicalSAM superfamily of proteins which use iron-sulfur clusters and SAM to initiate H atom abstraction reactions. Included in this unusual chemistry is the reductive cleavage of SAM to generate the...
متن کاملUtilization of S-adenosylmethionine by micro-organisms.
Shapiro, Stanley K. (Argonne National Laboratory, Argonne, Ill.). Utilization of S-adenosylmethionine by microorganisms. J. Bacteriol. 83:169-174. 1962.-Two types of mutants of Aerobacter aerogenes that utilize S-adenosylmethionine for growth are described. One type also responds to methionine, 5'methylthioadenosine, or a combination of homocysteine and S-methylmethionine. The second type of mu...
متن کاملStructural Basis for Putrescine Activation of Human S-Adenosylmethionine Decarboxylase†‡
Putrescine (1,4-diaminobutane) activates the autoprocessing and decarboxylation reactions of human S-adenosylmethionine decarboxylase (AdoMetDC), a critical enzyme in the polyamine biosynthetic pathway. In human AdoMetDC, putrescine binds in a buried pocket containing acidic residues Asp174, Glu178, and Glu256. The pocket is away from the active site but near the dimer interface; however, a ser...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)44724-7