Nucleotide sequence of gene celM encoding a new endoglucanase (CeIM) of Clostridium thermocellum and purification of the enzyme
Autor: | Ulf T. Gerngross, Arnold L. Demain, Patrick J. Barker, T. Kobayashi, M.P.M. Romaniec |
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Rok vydání: | 1993 |
Předmět: |
chemistry.chemical_classification
biology Structural gene Nucleic acid sequence biology.organism_classification Applied Microbiology and Biotechnology Molecular biology Stop codon Amino acid Open reading frame Biochemistry chemistry Codon usage bias Clostridium thermocellum Peptide sequence Biotechnology |
Zdroj: | Journal of Fermentation and Bioengineering. 76:251-256 |
ISSN: | 0922-338X |
DOI: | 10.1016/0922-338x(93)90189-f |
Popis: | The nucleotide sequence of a new endoglucanase gene ( celM ) of Clostridium thermocellum was determined. The structural gene contains an open reading frame of 978 by starting with an ATG codon and terminating in a TGA stop codon. The deduced amino acid sequence of endoglucanase M (CeIM) contains 325 amino acids (MW 35,186) and its N-terminal amino acid sequence is identical to that of the purified enzyme. The codon usage of the gene is similar to that of other endoglucanase genes in the same organism. The endoglucanase was purified from Escherichia coli with a 200-fold increase in specific activity. The optimum pH and temperature values of the enzyme are 5.5 to 6.5 and 60°C respectively for carboxymethylcellulose (CMC) degradation. |
Databáze: | OpenAIRE |
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