Hence, this enzyme has one substrate, (3S)-3,6-diaminohexanoate, and one product, (3S,5S)-3,5-diaminohexanoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is (3S)-3,6-diaminohexanoate 5,6-aminomutase. Other names in common use include beta-lysine mutase, and L-beta-lysine 5,6-aminomutase. This enzyme participates in lysine degradation. It employs one cofactor, cobamide.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1XRS.
Related Research Articles
Lysine 2,3-aminomutase is a radical SAM enzyme that facilitates the conversion of the amino acid lysine to beta-lysine. It accomplishes this interconversion using three cofactors and a 5'-deoxyadenosyl radical formed in a S-Adenosyl methionine (SAM) activated radical reaction pathway.[1] The generalized reaction is shown below:
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Stadtman TC, Renz P (1968). "Anaerobic degradation of lysine. V. Some properties of the cobamide coenzyme-dependent beta-lysine mutase of Clostridium sticklandii". Arch. Biochem. Biophys. 125 (1): 226–39. doi:10.1016/0003-9861(68)90657-7. PMID5649516.
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