.alpha.-amylase gene having ability for highly producing maltope

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

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43525233, 4353201, 536 232, C12W 928, C12W 120, C07H 2104, C12N 928, C12N 120, C12N 1500

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active

060871474

ABSTRACT:
A modified enzyme having a reduced maltopentaose decomposing activity and improvements in practical usability was provided by a gene coding for .alpha.-amylase highly producing maltopentaose, the .alpha.-amylase comprising an amino acid sequence where an amino acid residue at 57- or 139-position has been substituted in the amino acid sequence of maltopentaose-forming amylase derived from Pseudomonas sp. KO-8940 (Shida, O. et al., Biosci. Biotech. Biochem. Vol. 56, 76-80 (1992)).

REFERENCES:
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Rudinger (Jun. 1976) Characteristics of the amino acids as components of a peptide hormone sequence. In: Peptide Hormones. Ed. J. A. Parsons. University Park Press, Baltimore, MD. pp. 1-7.
Ngo et al. (Jan. 1994) Computational complexity, protein structure prediction, and the ILevinthal paradox. In: The Protein Folding Problem and Tertiary Structure Prediction. Eds. Merz et al. Birkhauser et al. Boston, MA. pp. 491-495.
Thornton et al. (Sep. 1995) Protein Engineering: Editorial Overview. Current Opinion in Biotechnology 6(4): 367-369.
Wallace (Apr. 1993) Understanding cytochrome c function: engineering protein structure by semisynthesis. The FASEB Journal 7: 505-515.
Osamu Shida, et al., Biosci. Biotech. Biochem., vol. 56, No. 1, pp. 76-80, "Cloning and Nucleotide Sequence of the Maltopentaose-Forming Amylase Gene from Pseudomonas SP. KO-8940", 1992.
Hisashi Okemoto, et al., Applied Microbiology and Biotechnology, vol. 25, pp. 137-142, "Isolation and Cultivation of a Novel Microorganism Producing a Maltopentaose-Forming Enzyme", 1986.

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