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Volumn 432, Issue 2, 2004, Pages 136-144
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Enantiospecific (+)- and (-)-germacrene D synthases, cloned from goldenrod, reveal a functionally active variant of the universal isoprenoid-biosynthesis aspartate-rich motif
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Author keywords
Enantiomers; Enantiospecificity; Germacrene D; Sesquiterpene; Solidago; Terpene cyclase
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Indexed keywords
ASPARTIC ACID;
COMPLEMENTARY DNA;
ENZYME;
GERMACRENE DEXTRO SYNTHASE;
ISOPRENOID;
MAGNESIUM;
SESQUITERPENE;
SOLIDAGO CANADENSIS EXTRACT;
UNCLASSIFIED DRUG;
AMINO ACID SEQUENCE;
ARTICLE;
ENANTIOMER;
ENANTIOSELECTIVITY;
ENZYME ACTIVITY;
ENZYME ISOLATION;
ENZYME STRUCTURE;
GENETIC VARIABILITY;
MOLECULAR CLONING;
MOLECULAR MODEL;
MUTAGENICITY;
NUCLEOTIDE SEQUENCE;
PLANT GENETICS;
PLANT INSECT INTERACTION;
PRIORITY JOURNAL;
PROTEIN MOTIF;
SOLIDAGO;
ALKYL AND ARYL TRANSFERASES;
AMINO ACID MOTIFS;
AMINO ACID SEQUENCE;
ASPARTIC ACID;
BINDING SITES;
CELLS, CULTURED;
CLONING, MOLECULAR;
COMPUTER SIMULATION;
ENZYME ACTIVATION;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN ENGINEERING;
RECOMBINANT PROTEINS;
SOLIDAGO;
STRUCTURE-ACTIVITY RELATIONSHIP;
SUBSTRATE SPECIFICITY;
TERPENES;
ESCHERICHIA COLI;
INSECTA;
SOLIDAGO;
SOLIDAGO CANADENSIS;
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EID: 7944232372
PISSN: 00039861
EISSN: None
Source Type: Journal
DOI: 10.1016/j.abb.2004.06.030 Document Type: Article |
Times cited : (71)
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References (42)
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