Two lysine residues are responsible for the enzymatic activities of indole prenyltransferases from fungi

ChemBioChem

Volumn 9, Issue 13, 2008, Pages 2055-2058

  Stec, Edyta ^a   Steffan, Nicola ^a   Kremer, Anika ^a   Zou, Huixi ^a,b   Zheng, Xiaodong ^b   Li, Shu Ming ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

^b ZHEJIANG UNIVERSITY   (China)

Author keywords

Aspergillus fumigatus; Biosynthesis; Indole prenyltransferases; Natural products; Site directed mutagenesis

Indexed keywords

ARGININE; ASPARTIC ACID; DIMETHYLALLYLTRANSFERASE; INDOLE; LYSINE; PRENYLAMINE; PYROPHOSPHATE;

ARTICLE; BINDING SITE; CATALYSIS; CHEMICAL BINDING; CONTROLLED STUDY; CRYSTALLIZATION; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; FUNGUS; MUTATION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ASPERGILLUS FUMIGATUS; DIMETHYLALLYLTRANSTRANSFERASE; FUNGI; INDOLES; LYSINE; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; MUTATION;

ASPERGILLUS FUMIGATUS; FUNGI;

EID: 54349115932     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.200800237     Document Type: Article

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