Hwang, KY Cho, CS Kim, SS Sung, HC Yu, YG Cho, YJ 2024-01-21T15:35:56Z 2024-01-21T15:35:56Z 2021-09-04 1999-05 1072-8368 https://pubs.kist.re.kr/handle/201004/142229 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 Angstrom 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. English NATURE PUBLISHING GROUP COMPLETE GENOME SEQUENCE AMINO-ACID RACEMASE MANDELATE RACEMASE CATALYTIC RESIDUES CRYSTAL-STRUCTURE ALANINE RACEMASE CARBON ACIDS ACTIVE-SITE PROTEIN IDENTIFICATION Structure and mechanism of glutamate racemase from Aquifex pyrophilus Article 1 NATURE STRUCTURAL BIOLOGY, v.6, no.5, pp.422 - 426 NATURE STRUCTURAL BIOLOGY 6 5 422 426 scie scopus 000080132600011 2-s2.0-0032915050 Biochemistry & Molecular Biology Biophysics Cell Biology Biochemistry & Molecular Biology Biophysics Cell Biology Letter COMPLETE GENOME SEQUENCE AMINO-ACID RACEMASE MANDELATE RACEMASE CATALYTIC RESIDUES CRYSTAL-STRUCTURE ALANINE RACEMASE CARBON ACIDS ACTIVE-SITE PROTEIN IDENTIFICATION crystal structure Aquifex pyrophilus glutamate racemase