| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1Institute of Molecular Genetics, Russian Academy of Science, Kurchatov Sq. 46, 123 182 Moscow, Russia
2Institute for Microbiology, Technical University of München, Arcisstr. 21, D-80290 München, Germany
3Author for correspondence: Wolfgang H. Schwarz. Tel: + 49 89 2892 2302. Fax: +49 89 2892 2360. e-mail: wolfgang.schwarz@mikro.biologie.tu-muenchen.de
ABSTRACT
The gene for thermostable 1,3-β-glucosidase BgIB was cloned from the chromosome of Thermotoga neapolitana and its primary sequence was determined. The purified recombinant β-glucosidase B had a monomer molecular mass of 81 kDa in accordance with the amino acid sequence predicted from the nucleotide sequence of clone pTT51. It was a member of glycosylhydrolase family 3 and belonged to enzyme class EC 3.2.1.21. β-Glucosidase B had a specific activity of 255 U mg-1on 4-nitrophenyl(PNP)-β-glucoside at the optima of pH (5.5) and temperature (90 °C), and Km values of 0.1, 10 and 50 mM for PNP-β-glucoside, laminaribiose and cellobiose, respectively. The gene bgIB was located immediately upstream of the laminarinase gene IamA. Both genes were transcribed from the same DNA strand and were not separated by a palindromic transcription terminator. The two purified enzymes 1,3-β-glucosidase BgIB (laminaribiase) and 1,3-β-glucanase LamA (laminarinase) were together capable of completely degrading laminarin to glucose.
Present address: Institute for Microbiology, Technical University of München, Arcisstr. 21, D-80290 München, Germany.
This article has been cited by other articles:
|
|
 |
|
  V. Aimanianda, C. Clavaud, C. Simenel, T. Fontaine, M. Delepierre, and J.-P. Latge Cell Wall {beta}-(1,6)-Glucan of Saccharomyces cerevisiae: STRUCTURAL CHARACTERIZATION AND IN SITU SYNTHESIS J. Biol. Chem., May 15, 2009; 284(20): 13401 - 13412. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. M. Nanavati, K. Thirangoon, and K. M. Noll Several Archaeal Homologs of Putative Oligopeptide-Binding Proteins Encoded by Thermotoga maritima Bind Sugars Appl. Envir. Microbiol., February 1, 2006; 72(2): 1336 - 1345. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. B. Conners, C. I. Montero, D. A. Comfort, K. R. Shockley, M. R. Johnson, S. R. Chhabra, and R. M. Kelly An Expression-Driven Approach to the Prediction of Carbohydrate Transport and Utilization Regulons in the Hyperthermophilic Bacterium Thermotoga maritima J. Bacteriol., November 1, 2005; 187(21): 7267 - 7282. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. K. McCarthy, A. Uzelac, D. F. Davis, and D. E. Eveleigh Improved Catalytic Efficiency and Active Site Modification of 1,4-{beta}-D-Glucan Glucohydrolase A from Thermotoga neapolitana by Directed Evolution J. Biol. Chem., March 19, 2004; 279(12): 11495 - 11502. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K.-P. Fuchs, V. V. Zverlov, G. A. Velikodvorskaya, F. Lottspeich, and W. H. Schwarz Lic16A of Clostridium thermocellum, a non-cellulosomal, highly complex endo-{beta}-1,3-glucanase bound to the outer cell surface Microbiology, April 1, 2003; 149(4): 1021 - 1031. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. Faure The Family-3 Glycoside Hydrolases: from Housekeeping Functions to Host-Microbe Interactions Appl. Envir. Microbiol., April 1, 2002; 68(4): 1485 - 1490. [Full Text] [PDF]
|
|
|
|
|
|
D. A. Yernool, J. K. McCarthy, D. E. Eveleigh, and J.-D. Bok Cloning and Characterization of the Glucooligosaccharide Catabolic Pathway beta -Glucan Glucohydrolase and Cellobiose Phosphorylase in the Marine Hyperthermophile Thermotoga neapolitana J. Bacteriol., September 15, 2000; 182(18): 5172 - 5179. [Abstract] [Full Text]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |
