Metal cofactors of lysine-2,3-aminomutase.
نویسندگان
چکیده
منابع مشابه
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...
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 کاملMetal-Carbon Bonds in Enzymes and Cofactors.
The occurrence of a wide variety of metal-carbon bonds in living organisms, ranging from bacteria to humans, is only recently recognized. Of course, the historical examples are the B12 coenzymes containing cobalt-carbon bonds, but now such bonds are also known for nickel, iron, copper, and other transition metal ions. There is no other comparable book; MILS-6, written by 17 experts, summarizes ...
متن کاملThe 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...
متن کاملS-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: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)89498-8