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PMID:15316858

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Citation

Ma, Y, Xue, Y, Dou, Y, Xu, Z, Tao, W and Zhou, P (2004) Characterization and gene cloning of a novel beta-mannanase from alkaliphilic Bacillus sp. N16-5. Extremophiles 8:447-54

Abstract

An alkaline beta-mannanase was purified to homogeneity from a culture broth of alkaliphilic Bacillus sp. N16-5. The enzyme had optimum activity at pH 9.5 and 70 degrees C. It was composed of a single polypeptide chain with a molecular weight of 55 kDa deduced from SDS-PAGE, and its isoelectric point was around pH 4.3. The enzyme efficiently hydrolyzed galactomannan and glucomannan, producing a series of oligosaccharides and monosaccharides. The beta-mannanase gene (manA) contained an open reading frame (ORF) of 1,479 bp, encoding a 32-amino acids signal peptide, and a mature protein of 461 amino acids, with a calculated molecular mass of 50,743 Da. Strain N16-5 ManA, deduced from the manA ORF, exhibited relatively high amino acid similarity to the members of the glycosyl hydrolase family 5. The eight conserved active-site amino acids in family 5 glycosyl hydrolase were found in the deduced amino acid sequence of strain N16-5 ManA.

Links

PubMed Online version:10.1007/s00792-004-0405-4

Keywords

Amino Acid Sequence; Bacillus/classification; Bacillus/enzymology; Bacillus/genetics; Base Sequence; Catalytic Domain/genetics; Cloning, Molecular; Conserved Sequence; DNA, Bacterial/genetics; Enzyme Stability; Genes, Bacterial; Hydrogen-Ion Concentration; Kinetics; Metals; Molecular Sequence Data; Molecular Weight; Open Reading Frames; Sequence Homology, Amino Acid; Substrate Specificity; Temperature; beta-Mannosidase/chemistry; beta-Mannosidase/genetics; beta-Mannosidase/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

9BACI:Q5YEX6

enables

GO:0004567: beta-mannosidase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

9BACI:Q5YEX6

GO:0004567: beta-mannosidase activity

ECO:0000314:

F

This mannanse was examined for its ability to hydrolyze various substrates. This table shows this enzyme was specific toward bB1,4- mannosidic linkages of mannopolysaccharides

complete
CACAO 9798

See also

References

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