Structural and biochemical characterization of the Escherichia coli argE gene product.

Abstract:

:The DNA sequence of a 2,100-bp region containing the argE gene from Escherichia coli has been determined. The nucleotide sequence of the ppc-argE intergenic region was also solved and shown to contain six tandemly repeated REP sequences. Moreover, the oxyR gene has been mapped on the E. coli chromosome and shown to flank the arg operon. The codon responsible for the translation start of argE was determined by using site-directed mutants. This gene spans 1,400 bp and encodes a 42,350-Da polypeptide. The argE3 allele and a widely used argE amber gene have also been cloned and sequenced. N-Acetylornithinase, the argE product, has been overproduced and purified to homogeneity. Its main biochemical and catalytic properties are described. Moreover, we demonstrate that the protein is composed of two identical subunits. Finally, the amino acid sequence of N-acetylornithinase is shown to display a high degree of identity with those of the succinyldiaminopimelate desuccinylase from E. coli and carboxypeptidase G2 from a Pseudomonas sp. It is proposed that this carboxypeptidase might be responsible for the acetylornithinase-related activity found in the Pseudomonas sp.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Meinnel T,Schmitt E,Mechulam Y,Blanquet S

doi

10.1128/jb.174.7.2323-2331.1992

keywords:

subject

Has Abstract

pub_date

1992-04-01 00:00:00

pages

2323-31

issue

7

eissn

0021-9193

issn

1098-5530

journal_volume

174

pub_type

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