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(Received for publication, March 22, 1996, and in revised form, August 19, 1996)
From the Department of Biology and the McCollum-Pratt Institute,
The Johns Hopkins University, Baltimore, Maryland 21218
The accompanying papers (Keyhani, N. O., and
Roseman, S. (1996) J. Biol. Chem. 271, 33414-33424;
Keyhani, N. O., and Roseman, S. (1996) J. Biol. Chem. 271, 33425-33432) describe two unique The predicted protein sequence is unique among
Volume 271, Number 52,
Issue of December 27, 1996
pp. 33433-33439
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-N-Acetyl-D-glucosaminidase from
Vibrio furnissii
-N-acetylglucosaminidases from Vibrio
furnissii. A third, ExoII, is reported here. The gene,
exoII, was cloned into Escherichia coli,
sequenced, and ExoII purified to apparent homogeneity (36 kDa). The
molecular weight and N-terminal 16 amino acids of the protein conform
to the predicted sequence. ExoII exhibited unique substrate
specificity. It rapidly cleaved p-nitrophenyl and
4-methylumbelliferyl -GlcNAc, was slightly active with
p-nitrophenyl--GalNAc, and was inactive with all other
GlcNAc derivatives tested, including N,N
-diacetylchitobiose and (GlcNAc)n,
n = 3-6. Unlike GlcNAc (Ki, 210 µM), (GlcNAc)n are poor inhibitors of ExoII.
-N-acetylglucosaminidases excepting Cht60, recently
cloned from a marine Alteromonas (Tsujibo, H., Fujimoto,
K., Tanno, H., Miyamoto, K., Imada, C., Okami, Y., and Inamori, Y. (1994) Gene (Amst.) 146, 111-115). Cht60, a
chitobiase, is 26.9% identical to ExoII in a 182-amino acid overlap,
but the two enzymes differ in substrate specificity and other
properties. ExoII shares similarity with five bacterial and yeast
-glucosidases, up to 44% identity in the 25-amino acid catalytic
domain. By analogy, ExoII may play a role in signal transduction
between invertebrate hosts and V. furnissii.
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