TOP > Available Issues > Table of Contents > Abstract
| | ONLINE | ISSN | : | 1347-6947 | | PRINT | ISSN | : | 0916-8451 |
|
| | Bioscience, Biotechnology, and Biochemistry |
| Vol. 64 (2000) , No. 11 pp.2281-2289 |
| [Image PDF (1738K)] [References]  |
 | Deduced Amino Acid Sequence and Possible Catalytic Residues of a Thermostable, Alkaline Cellulase from an Alkaliphilic Bacillus Strain
|
| | | 1) Tochigi Research Laboratories of Kao Corporation |
| (Received December 16, 1999)
(Accepted June 23, 2000)
|
| | Alkaliphilic Bacillus sp. strain KSM-S237 (a relative of Bacillus pseudofirmus) produces a thermostable, alkaline endo-1,4-β-glucanase (Egl). The entire gene for the enzyme harbored a 2,472-bp open reading frame (ORF) encoding 824 amino acids, including a 30-amino-acid signal peptide. The deduced amino acid sequence of the mature enzyme (794 amino acids, 88,284 Da) showed very high similarity to those of family 5 mesophilic, alkaline Egls from some alkaliphilic bacilli. The enzyme had a region similar to a novel cellulose binding domain proposed for an Egl (EngF) from Clostridium cellulovorans. Expression of the Bacillus Egl gene in Bacillus subtilis resulted in high carboxymethy cellulase activity (2.0 g/l) in the culture broth, concomitant with the appearance of a protein band on an SDS gel at 86 kDa. Site-directed mutagenesis delineated the importance of Arg111, His151, Glu190, His262, Tyr264, and Glu305 in catalysis and/or substrate binding of the enzyme.
|
| | | |
| To cite this article: | | Yoshihiro HAKAMADA, Yuji HATADA, Kenzo KOIKE, Tadashi YOSHIMATSU, Shuji KAWAI, Tohru KOBAYASHI and Susumu ITO, “Deduced Amino Acid Sequence and Possible Catalytic Residues of a Thermostable, Alkaline Cellulase from an Alkaliphilic Bacillus Strain”, Biosci. Biotechnol. Biochem., Vol. 64, 2281-2289 (2000) . | |
|
| doi:10.1271/bbb.64.2281 | | JOI JST.JSTAGE/bbb/64.2281 |
| Copyright (c) 2005 by Japan Society for Bioscience, Biotechnology, and Agrochemistry |
|
|
