Amino-acid racemase

Last updated
amino-acid racemase
Identifiers
EC no. 5.1.1.10
CAS no. 9068-61-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, an amino-acid racemase (EC 5.1.1.10) is an enzyme that catalyzes the chemical reaction

an L-amino acid a D-amino acid

Hence, this enzyme has one substrate, L-amino acid, and one product, D-amino acid.

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is amino-acid racemase. This enzyme is also called L-amino acid racemase. This enzyme participates in 4 metabolic pathways: glycine, serine and threonine metabolism, cysteine metabolism, D-glutamine and D-glutamate metabolism, and D-arginine and D-ornithine metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2FKP, 2GGG, 2GGH, 2GGI, and 2GGJ.

Related Research Articles

Pyridoxal phosphate Active formof vitamin B6

Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates.

Methylmalonyl CoA epimerase

Methylmalonyl CoA epimerase is an enzyme involved in fatty acid catabolism that is encoded in human by the "MCEE" gene located on chromosome 2. It is routinely and incorrectly labeled as "methylmalonyl-CoA racemase". It is not a racemase because the CoA moiety has 5 other stereocenters.

Epimerases and racemases are isomerase enzymes that catalyze the inversion of stereochemistry in biological molecules. Racemases catalyze the stereochemical inversion around the asymmetric carbon atom in a substrate having only one center of asymmetry. Epimerases catalyze the stereochemical inversion of the configuration about an asymmetric carbon atom in a substrate having more than one center of asymmetry, thus interconverting epimers.

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References