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The gene encoding a
Volume 270,
Number 15,
Issue of April 14, pp. 8805-8814, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
- N-Acetylglucosaminidase Gene from Streptococcus
pneumoniae
GENERATION OF TRUNCATED ENZYMES WITH MODIFIED AGLYCON
SPECIFICITY
- N-acetylglucosaminidase from
Streptococcus pneumoniae has been obtained by screening an
expression library for - N-acetylglucosaminidase activity.
Clones of different nucleotide sizes each having arylglycoside activity
were obtained, and DNA sequencing revealed a gene of 3933 base pairs
possessing typical bacterial transcription initiation and termination
sequences and terminating in an ochre stop codon. Computer analysis of
the translated protein of 1311 amino acids (144,210 Da) identified a
tandem repeat within which lies a sequence homologous with six other
hexosaminidase gene products from a wide variety of species ranging
from bacteria to humans. Also found were an amino-terminal putative
secretion signal peptide and a carboxyl-terminal cell sorting/anchorage
motif typically found in over 20 other Gram-positive surface proteins.
The expression of an almost complete DNA clone in Escherichia coli produced a functional and authentic
- N-acetylglucosaminidase with aglycon specificity
identical to the wild-type enzyme. However, enzymes produced from
truncated DNA clones show more restricted aglycon specificity and are
unable to hydrolyze terminal 1-2GlcNAc residues from
N-glycans containing a bisecting N-acetylglucosamine.
The availability of these clones allows structural analyses to be made
of catalytic and oligosaccharide recognition protein domains that
enhance functional activity.
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