PMID:10331867

Citation	Hwang, KY, Cho, CS, Kim, SS, Sung, HC, Yu, YG and Cho, Y (1999) Structure and mechanism of glutamate racemase from Aquifex pyrophilus. Nat. Struct. Biol. 6:422-6
Abstract	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.
Links	PubMed Online version:10.1038/8223
Keywords	Amino Acid Isomerases/chemistry; Amino Acid Isomerases/genetics; Amino Acid Isomerases/metabolism; Amino Acid Sequence; Amino Acid Substitution; Apoenzymes/chemistry; Apoenzymes/metabolism; Binding Sites; Catalysis; Crystallography, X-Ray; Cysteine/chemistry; Cysteine/metabolism; Dimerization; Glutamine/chemistry; Glutamine/metabolism; Gram-Negative Aerobic Rods and Cocci/enzymology; Gram-Negative Aerobic Rods and Cocci/genetics; Kinetics; Models, Chemical; Models, Molecular; Molecular Sequence Data; Phosphopyruvate Hydratase/chemistry; Protein Binding; Protein Conformation; Protein Structure, Secondary
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
AQUPY:MURI		GO:0008881: glutamate racemase activity	ECO:0000315:		F		Structural and mutational analysis allows us to propose a mechanism of metal cofactor-independent glutamate racemase in which 2 cysteine residues are involved in catalysis.	complete CACAO 4798

References

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