Previous Article | Next Article ![]()
Applied and Environmental Microbiology, August 1998, p. 2920-2924, Vol. 64, No. 8
Osaka University of Pharmaceutical Sciences,
4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan
Received 16 March 1998/Accepted 22 May 1998
A
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
A Novel
-N-Acetylglucosaminidase from
Streptomyces thermoviolaceus OPC-520: Gene Cloning,
Expression, and Assignment to Family 3 of the Glycosyl
Hydrolases
-N-acetylglucosaminidase gene (nagA)
of Streptomyces thermoviolaceus OPC-520 was cloned in
Streptomyces lividans 66. The nucleotide sequence of the
gene, which encodes NagA, revealed an open reading frame of 1,896 bp,
encoding a protein with an Mr of 66,329. The
deduced primary structure of NagA was confirmed by comparison with the
N-terminal amino acid sequence of the cloned
-N-acetylglucosaminidase expressed by S. lividans. The enzyme shares no sequence similarity with the
classical
-N-acetylglucosaminidases belonging to family
20. However, NagA, which showed no detectable
-glucosidase activity,
revealed homology with microbial
-glucosidases belonging to family
3; in particular, striking homology with the active-site regions of
-glucosidases was observed. Thus, the above-mentioned results
indicate that NagA from S. thermoviolaceus OPC-520 is
classified as a family 3 glycosyl hydrolase. The enzyme activity was
optimal at 60°C and pH 5.0, and the apparent
Km and Vmax values for
p-nitrophenyl-
-N-acetylglucosamine were
425.7 µM and 24.8 µmol min
1 mg of
protein
1, respectively.
*
Corresponding author. Mailing address: Osaka University
of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan. Phone and fax: (81-726) 90-1057. E-mail:
tsujibo{at}oysun01.oups.ac.jp.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»