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Volumn 17, Issue 2, 2016, Pages 132-136
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Active-Site Engineering Expands the Substrate Profile of the Basidiomycete l -Tryptophan Decarboxylase CsTDC
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Author keywords
amino acids; basidiomycete; enzymes; protein engineering; tryptophan decarboxylase
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Indexed keywords
5 HYDROXYTRYPTOPHAN;
AROMATIC LEVO AMINO ACID DECARBOXYLASE;
LEVODOPA;
TRYPTOPHAN;
TYROSINE DECARBOXYLASE;
AMINO ACID SUBSTITUTION;
ARTICLE;
BINDING AFFINITY;
CERIPORIOPSIS SUBVERMISPORA;
DECARBOXYLATION;
ENZYME ACTIVE SITE;
ENZYME ENGINEERING;
ENZYME SPECIFICITY;
FUNGAL BIOMASS;
IN VITRO STUDY;
MUTAGENESIS;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN EXPRESSION;
PROTEIN MOTIF;
STEREOSPECIFICITY;
BASIDIOMYCETES;
CHEMICAL STRUCTURE;
CHEMISTRY;
ENZYMOLOGY;
GENETIC VARIATION;
GENETICS;
HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;
PROTEIN ENGINEERING;
AROMATIC-L-AMINO-ACID DECARBOXYLASES;
BASIDIOMYCOTA;
CATALYTIC DOMAIN;
CHROMATOGRAPHY, HIGH PRESSURE LIQUID;
GENETIC VARIATION;
MOLECULAR STRUCTURE;
PROTEIN ENGINEERING;
SUBSTRATE SPECIFICITY;
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EID: 84954527638
PISSN: 14394227
EISSN: 14397633
Source Type: Journal
DOI: 10.1002/cbic.201500438 Document Type: Article |
Times cited : (27)
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References (14)
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