Affiliation:
1. Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111
Abstract
ABSTRACT
The β-
N
-acetylglucosaminidase of
Escherichia coli
was found to have a novel specificity and to be encoded by a gene (
nagZ
) that maps at 25.1 min. It corresponds to an open reading frame,
ycfO
, whose predicted amino acid sequence is 57% identical to that of
Vibrio furnissii
ExoII. NagZ hydrolyzes the β-1,4 glycosidic bond between
N
-acetylglucosamine and
anhydro-N
-acetylmuramic acid in cell wall degradation products following their importation into the cell during the process for recycling cell wall muropeptides. From amino acid sequence comparisons, the novel β-
N
-acetylglucosaminidase appears to be conserved in all 12 gram-negative bacteria whose complete or partial genome sequence data are available.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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