Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. Organization of the mut genes.
The gene encoding component E, the large subunit, of adenosylcobalamin (coenzyme B12)-dependent glutamate mutase from Clostridium tetanomorphum has been cloned and sequenced. The mutE gene encodes a protein of 485 amino acid residues, with M(r) 53,708. The mutE gene is situated some 1,400 bp downstream of the mutS gene, which encodes the small subunit of glutamate mutase. Between the two is an open reading frame encoding a protein of 462 amino acids, with M(r) 50,171, and of unknown function. All three genes appear to be transcribed as an operon and lie immediately upstream of the gene encoding beta-methylaspartase, the next enzyme in the pathway of glutamate fermentation. Local homology exists between mutE and a region of beta-methylaspartase which contains an active-site serine residue.
Holloway
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Department of Biochemistry, University of Cambridge, UK.
Marsh
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EN
D000591:Amino Acid Isomerases / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003013:Clostridium / Q000201:enzymology*; D004269:DNA, Bacterial; D005798:Genes, Bacterial; D019751:Intramolecular Transferases; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D004269:DNA, Bacterial; D000591:Amino Acid Isomerases; D019751:Intramolecular Transferases; C021570:methylaspartate mutase