Lysine 2,3-Aminomutase

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Metal 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...

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Mechanistic 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...

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The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale.

The x-ray crystal structure of the pyridoxal-5'-phosphate (PLP), S-adenosyl-L-methionine (SAM), and [4Fe-4S]-dependent lysine-2,3-aminomutase (LAM) of Clostridium subterminale has been solved to 2.1-A resolution by single-wavelength anomalous dispersion methods on a L-selenomethionine-substituted complex of LAM with [4Fe-4S]2+, PLP, SAM, and L-alpha-lysine, a very close analog of the active Mic...

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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...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1989

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)94194-3