Method of altering enzymes and a novel neopullulanase

Chemistry: molecular biology and microbiology – Process of mutation – cell fusion – or genetic modification – Introduction of a polynucleotide molecule into or...

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435 691, 435193, 435201, 435210, 4352523, 4353201, 435476, 536 232, C12N 1511, C12N 1554, C12N 1556, C12N 1570

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059654422

ABSTRACT:
An enzyme is altered by introducing an additional hydrophobic group to enhance the hydrophobic environment in the enzyme so as to interfere with entrance of a water molecule. In this connection, the site of introduction and kind of hydrophobic group to be introduced are selected on the basis of comprehensive analysis of amino acid sequence, three-dimensional structure, reaction mechanism or the like of the target enzyme. Using this method, an amino acid residue of neopullulanase derived from Bacillus stearothermophilus was replaced by another amino acid.

REFERENCES:
patent: 4853871 (1989-08-01), Pantoliano et al.
patent: 5162210 (1992-11-01), Sierks et al.
patent: 5166741 (1992-11-01), Bryan et al.
patent: 5352594 (1994-10-01), Poulouse
Kuriki, T., et al., Journal of Bacteriology, vol. 173, "Analysis of the active center of Bacillus stearothermophilus neopullulanase", pp. 6147-6152, 1991.
"Action of Neopullulanase," J. Biol. Chem. 267:18447-18452 (Sep. 15, 1992).
Rastetter (1983) Trends Biotech 1:80-84. "Enzyme engineering: applications and promise".
Lamminmaki et al (1996) Bioc. Biop. Acta 1295:195-200. "Structual consequences of neopullulanase mutations".
Matsui et al (1994) Biochem 33:451-458 "Roles of the aromatic residues conserved in the active center of Saccharomycopsis .alpha.-anylase for transglycosylation and Hydrolysis Activity".
Kuriki et al (1996) JBC 271:17321-17329 "Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint . . . ".
Mosimann et al (1995) proteins: structure, function and genetics 23:301-317 "A critical assessment of comparative molecular modeling of tertiary structure of proteins".
"Hydrophobic parameters of .pi. of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides," Jean-Luc Fauchere, et al., Eur. J. Med. Chem. --Chim. Ther., 1983-18, No. 4, pp. 369-375.

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