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Volumn 39, Issue 44, 2000, Pages 13350-13355
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Removal of the four C-terminal glycine-rich repeats enhances the thermostability and substrate binding affinity of barley β-amylase
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Author keywords
[No Author keywords available]
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Indexed keywords
BETA AMYLASE;
GLYCINE;
STARCH;
ARTICLE;
BARLEY;
BINDING AFFINITY;
CARBOXY TERMINAL SEQUENCE;
ENZYME DEGRADATION;
ENZYME STABILITY;
ENZYME STRUCTURE;
ENZYME SUBSTRATE COMPLEX;
GENE DELETION;
GERMINATION;
NONHUMAN;
PRIORITY JOURNAL;
THERMOSTABILITY;
AMINO ACID SEQUENCE;
BETA-AMYLASE;
BINDING SITES;
ENZYME STABILITY;
GLYCINE;
HEAT;
HORDEUM;
HYDROLYSIS;
KINETICS;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
PEPTIDE FRAGMENTS;
RECOMBINANT PROTEINS;
REPETITIVE SEQUENCES, AMINO ACID;
SEQUENCE DELETION;
STARCH;
SUBSTRATE SPECIFICITY;
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EID: 0034619496
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi000688s Document Type: Article |
Times cited : (38)
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References (23)
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