Isolation of the murI gene from Brevibacterium lactofermentum ATCC 13869 encoding D-glutamate racemase.
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.
Malathi
K C
KC
Department of Bioengineering, Tokyo Institute of Technology, Yokohama, Japan.
Wachi
M
M
Nagai
K
K
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
D000591:Amino Acid Isomerases; C062292:glutamate racemase