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Volumn 16, Issue 1, 1997, Pages 11-17
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Cysteine 265 is in the active site of, but is not essential for catalysis by tRNA-guanine transglycosylase (TGT) from Escherichia coli
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Author keywords
chemical modification; cysteine; mutagenesis; Queuine; tRNA modification
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Indexed keywords
5,5' DITHIOBIS(2 NITROBENZOIC ACID);
CYSTEINE;
GLYCOSYLTRANSFERASE;
GUANINE;
MESYLIC ACID METHYL ESTER;
METALLOPROTEIN;
N ETHYLMALEIMIDE;
QUEUINE;
THIOL REAGENT;
TRANSFER RNA;
ZINC;
ABSORPTION SPECTROSCOPY;
ARTICLE;
CATALYSIS;
CHEMICAL MODIFICATION;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME STRUCTURE;
ESCHERICHIA COLI;
NONHUMAN;
SITE DIRECTED MUTAGENESIS;
ZYMOMONAS MOBILIS;
BINDING SITES;
CATALYSIS;
CIRCULAR DICHROISM;
CYSTEINE;
DITHIONITROBENZOIC ACID;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
ENZYME ACTIVATION;
ESCHERICHIA COLI;
KINETICS;
MUTATION;
PENTOSYLTRANSFERASES;
TITRIMETRY;
ESCHERICHIA COLI;
GARCIA;
ZYMOMONAS MOBILIS;
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EID: 0031058577
PISSN: 02778033
EISSN: None
Source Type: Journal
DOI: 10.1023/A:1026334726357 Document Type: Article |
Times cited : (3)
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References (15)
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