Glutamate 2,3-aminomutase
Class of enzymes / From Wikipedia, the free encyclopedia
Glutamate 2,3-aminomutase (EC 5.4.3.9) is an enzyme that belongs to the radical s-adenosyl methionine (SAM) superfamily. Radical SAM enzymes facilitate the reductive cleavage of S-adenosylmethionine (SAM) through the use of radical chemistry and an iron-sulfur cluster.[1] This enzyme family is implicated in the biosynthesis of DNA precursors, vitamin, cofactor, antibiotic and herbicides and in biodegradation pathways.[1] In particular, glutamate 2,3 aminomutase is involved in the conversion of L-alpha-glutamate to L-beta-glutamate in Clostridium difficile.[2] The generalized reaction is shown below:
This enzyme is closely related to Lysine 2,3-aminomutase (LAM) and is thought to use similar cofactors and has a similar reaction mechanism. Experimental evidence suggests that glutamate 2,3 aminomutase uses a pyridoxal 5-phosphate cofactor to catalyze the reaction shown. The pyridoxal 5-phosphate cofactor (Vitamin B6) is heavily utilized by enzymes that catalyze aminoacid transformations.[3]