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Volumn 268, Issue 14, 2001, Pages 3974-3982
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Deduced amino-acid sequence of a calcium-free α-amylase from a strain of Bacillus: Implications from molecular modeling of high oxidation stability and chelator resistance of the enzyme
a
KAO CORPORATION
(Japan)
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Author keywords
amylase; Amino acid sequence; Bacillus; Molecular modeling; Oxidative stability
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Indexed keywords
AMINO ACID;
AMYLASE;
CALCIUM;
CHELATING AGENT;
ENZYME;
LEUCINE;
LIGAND;
METHIONINE;
NUCLEOTIDE;
SIGNAL PEPTIDE;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ARTICLE;
BACILLUS AMYLOLIQUEFACIENS;
BACILLUS LICHENIFORMIS;
CHELATION;
CONTROLLED STUDY;
ENZYME DEGRADATION;
ENZYME LOCALIZATION;
ENZYME STABILITY;
ENZYME STRUCTURE;
GENETIC CODE;
GEOBACILLUS STEAROTHERMOPHILUS;
GEOMETRY;
MOLECULAR MODEL;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
OPEN READING FRAME;
OXIDATION;
PRIORITY JOURNAL;
SEQUENCE HOMOLOGY;
ALKALIES;
ALPHA-AMYLASE;
AMINO ACID SEQUENCE;
BACILLUS;
BASE SEQUENCE;
CALCIUM;
CATIONS;
CHELATING AGENTS;
ENZYME STABILITY;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
OXIDATION-REDUCTION;
SEQUENCE HOMOLOGY, AMINO ACID;
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EID: 0034836495
PISSN: 00142956
EISSN: None
Source Type: Journal
DOI: 10.1046/j.1432-1327.2001.02308.x Document Type: Article |
Times cited : (30)
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References (32)
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