Structural highlights
Function
[MURI_AQUPY] Provides the (R)-glutamate required for cell wall biosynthesis. Converts L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Glutamate racemase (MurI) is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls. The crystal structure of glutamate racemase from Aquifex pyrophilus, determined at 2.3 A resolution, reveals that the enzyme forms a dimer and each monomer consists of two alpha/beta fold domains, a unique structure that has not been observed in other racemases or members of an enolase superfamily. A substrate analog, D-glutamine, binds to the deep pocket formed by conserved residues from two monomers. The structural and mutational analyses allow us to propose a mechanism of metal cofactor-independent glutamate racemase in which two cysteine residues are involved in catalysis.
Structure and mechanism of glutamate racemase from Aquifex pyrophilus.,Hwang KY, Cho CS, Kim SS, Sung HC, Yu YG, Cho Y Nat Struct Biol. 1999 May;6(5):422-6. PMID:10331867[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hwang KY, Cho CS, Kim SS, Sung HC, Yu YG, Cho Y. Structure and mechanism of glutamate racemase from Aquifex pyrophilus. Nat Struct Biol. 1999 May;6(5):422-6. PMID:10331867 doi:10.1038/8223
