Molecular cloning, characterization and purification of ornithine carbamoyltransferase from Mycobacterium bovis BCG.
Mol Gen Genet
; 234(3): 475-80, 1992 Sep.
Article
em En
| MEDLINE
| ID: mdl-1406593
ABSTRACT
A genomic library of Mycobacterium bovis BCG has been constructed by cloning DNA partially digested with Sau3A into the Escherichia coli expression vector pAS1. The gene coding for ornithine carbamoyl-transferase (EC.2.1.3.3; OTCase), hereafter referred to as argF, was isolated from the library by complementation of a double argF-argI mutant of E. coli and its sequence was determined. The translation initiation codon used, GTG, was identified by comparing the amino acid sequence deduced from the gene with the N-terminal sequence of the corresponding purified protein. On this basis, the M. bovis BCG OTCase monomer consists of 307 amino acid residues and displays about 44% identity with other OTCases, the most closely related homologue being the anabolic enzyme of Pseudomonas aeruginosa. The native enzyme has an estimated molecular mass of 110 kDa, suggesting a trimeric structure as is the case for most of the anabolic OTCases known from various organisms.
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Base de dados:
MEDLINE
Assunto principal:
Ornitina Carbamoiltransferase
/
Genes Bacterianos
/
Mycobacterium bovis
Idioma:
En
Ano de publicação:
1992
Tipo de documento:
Article