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Volumn 501, Issue 2-3, 2001, Pages 106-110
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Oligosaccharyltransferase is highly specific for the hydroxy amino acid in Asn-Xaa-Thr/Ser
a a a a a |
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Author keywords
Enzyme kinetics; Hydrophobic binding site; Oligosaccharyltransferase; Stereospecificity; Threonine analogue
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Indexed keywords
AMIDE;
ASPARAGINE;
BETA HYDROXYNORLEUCINE;
BETA,GAMMA DIAMINOBUTANOIC ACID;
CYSTEINE;
DIAMINOBUTYRIC ACID;
GLYCAN DERIVATIVE;
HYDROXYAMINO ACID;
METHYL GROUP;
NORLEUCINE;
NORVALINE;
OLIGOSACCHARYLTRANSFERASE;
SERINE;
THREO BETA HYDROXYNORVALINE;
THREONINE;
TRANSFERASE;
TRIPEPTIDE;
UNCLASSIFIED DRUG;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ARTICLE;
BINDING SITE;
CONFORMATION;
ENZYME ACTIVITY;
ENZYME BINDING;
ENZYME GLYCOSYLATION;
ENZYME SPECIFICITY;
PEPTIDE SYNTHESIS;
PH;
PRECURSOR;
PRIORITY JOURNAL;
STEREOSPECIFICITY;
SURFACE CHARGE;
ANIMALS;
BINDING SITES;
CATALYSIS;
GLYCOSYLATION;
HEXOSYLTRANSFERASES;
MEMBRANE PROTEINS;
MOLECULAR CONFORMATION;
PEPTIDES;
SUBSTRATE SPECIFICITY;
SWINE;
TRANSFERASES;
SUS SCROFA;
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EID: 0035919722
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(01)02641-2 Document Type: Article |
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Times cited : (24)
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References (17)
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