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Volumn 40, Issue 6, 2001, Pages 1844-1849
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N-terminal intramolecularly conserved histidines of three domains in Gonylaulax luciferase are responsible for loss of activity in the alkaline region
a,b
a
a,c
d
a
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Author keywords
[No Author keywords available]
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Indexed keywords
HISTIDINE DERIVATIVE;
HYBRID PROTEIN;
LUCIFERASE;
ALKALINITY;
AMINO ACID SUBSTITUTION;
AMINO TERMINAL SEQUENCE;
ARTICLE;
BIOLUMINESCENCE;
DINOFLAGELLATE;
ENZYME ACTIVITY;
ENZYME CONFORMATION;
ESCHERICHIA COLI;
GENETIC CONSERVATION;
NONHUMAN;
PH;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
PROTEIN DOMAIN;
PROTEIN EXPRESSION;
REGULATORY MECHANISM;
SITE DIRECTED MUTAGENESIS;
AMINO ACID SEQUENCE;
ANIMALS;
CONSERVED SEQUENCE;
DINOFLAGELLIDA;
ENZYME ACTIVATION;
GLUTATHIONE TRANSFERASE;
HISTIDINE;
HYDROGEN-ION CONCENTRATION;
LUCIFERASES;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
PEPTIDE FRAGMENTS;
PLASMIDS;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT FUSION PROTEINS;
SEQUENCE DELETION;
DINOPHYCEAE;
ESCHERICHIA COLI;
GONYAULAX;
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EID: 0035852837
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi002094v Document Type: Article |
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Times cited : (20)
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References (18)
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