title: Isolation of the murI gene from Brevibacterium lactofermentum ATCC 13869 encoding D-glutamate racemase.
abstract: The murI gene encoding D-glutamate racemase plays an important role in the biosynthesis of D-glutamic acid, an essential component of cell wall peptidoglycan of almost all eubacteria. A DNA fragment that could rescue the auxotrophy of D-glutamic acid in the Escherichia coli murI mutant strain WM335 was isolated from Brevibacterium lactofermentum ATCC 13869 belonging to the coryneform bacteria. DNA sequencing reveals that it encodes a protein of 284 amino acid residues, which shows a high level of homology with D-glutamate racemases from several other bacteria.
authors.affiliation: Department of Bioengineering, Tokyo Institute of Technology, Yokohama, Japan.
authors.forename: K C
authors.initials: KC
authors.lastname: Malathi
authors.forename: M
authors.initials: M
authors.lastname: Wachi
authors.forename: K
authors.initials: K
authors.lastname: Nagai
mesh_terms: D000591:Amino Acid Isomerases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D000595:Amino Acid Sequence; D001951:Brevibacterium / Q000201:enzymology / Q000235:genetics*; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
chemical_list: D000591:Amino Acid Isomerases; C062292:glutamate racemase