Abstract
The complete sequence of a beta-mannanase gene from an anaerobic extreme thermophile was determined, and it shows that the expressed protein consists of two catalytic domains and two binding domains separated by spacer regions rich in proline and threonine residues. The amino-terminal catalytic domain has beta-mannanase activity, and the carboxy-terminal domain acts as an endoglucanase. Neither domain shows homology with any other cellulase or hemicellulase sequence at the nucleic acid or protein level.
MeSH Terms
Amino Acid Sequence
Bacteria, Anaerobic/enzymology,genetics
Base Sequence
Cellulase/genetics
DNA, Bacterial/genetics
Mannosidases/genetics
Molecular Sequence Data
Multienzyme Complexes/genetics
Protein Conformation
Sequence Homology, Amino Acid
beta-Mannosidase
Chemicals
DNA, Bacterial
Multienzyme Complexes
Mannosidases
beta-Mannosidase
Cellulase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Gibbs M D
Department of Cellular & Molecular Biology, University of Auckland, New Zealand.
Saul D J
Lüthi E
Bergquist P L
References (10)
10 references, click to expand
-
Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
Microbiol Rev. 1991 Jun;55(2):303-15
PMID: 1886523
-
Two Bacillus beta-mannanases having different COOH termini are produced in Escherichia coli carrying pMAH5.
Appl Environ Microbiol. 1989 Dec;55(12):3178-83
PMID: 2694961
-
Structure of a Bacillus subtilis endo-beta-1,4-glucanase gene.
Nucleic Acids Res. 1986 Nov 25;14(22):9159-70
PMID: 3024130
-
Use of Congo red-polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from the bovine rumen.
Appl Environ Microbiol. 1982 Apr;43(4):777-80
PMID: 7081984
-
Nucleotide sequence of a cellulase gene of Bacillus subtilis.
Eur J Biochem. 1987 Apr 15;164(2):317-20
PMID: 3106035
-
Hemicellulases of Bacillus species: preliminary comparative studies on production and properties of mannanases and galactanases.
J Appl Bacteriol. 1990 Mar;68(3):253-61
PMID: 2111303
-
celB, a gene coding for a bifunctional cellulase from the extreme thermophile "Caldocellum saccharolyticum".
Appl Environ Microbiol. 1990 Oct;56(10):3117-24
PMID: 2126700
-
Lambda ZAP: a bacteriophage lambda expression vector with in vivo excision properties.
Nucleic Acids Res. 1988 Aug 11;16(15):7583-600
PMID: 2970625
-
Inducible expression vectors incorporating the Escherichia coli atpE translational initiation region.
Gene. 1987;52(2-3):279-83
PMID: 3038690
-
Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for a beta-mannanase from the extremely thermophilic bacterium "Caldocellum saccharolyticum".
Appl Environ Microbiol. 1991 Mar;57(3):694-700
PMID: 2039230