Structures of two natural product rnethyltransferases reveal the basis for substrate specificity in plant o-methyltransferases

Nature Structural Biology

Volumn 8, Issue 3, 2001, Pages 271-279

  Zubieta, Chloe ^a   He, Xian Zhi ^b   Dixon, Richard A ^b   Noel, Joseph P ^a  

^a SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^b PLANT BIOLOGY DIVISION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHALCONE DERIVATIVE; ISOFLAVONE DERIVATIVE; ISOLIQUIRITIGENIN; METHYLTRANSFERASE; NATURAL PRODUCT; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE;

ALFALFA; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN METABOLISM; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BINDING SITES; CATECHOL O-METHYLTRANSFERASE; CHALCONE; CHALCONES; CHROMATOGRAPHY, THIN LAYER; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HISTIDINE; HYDROXYLATION; ISOFLAVONES; MEDICAGO SATIVA; METHYLTRANSFERASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; S-ADENOSYLHOMOCYSTEINE; SEQUENCE ALIGNMENT; SITE-SPECIFIC DNA METHYLTRANSFERASE (CYTOSINE-SPECIFIC); SUBSTRATE SPECIFICITY;

MEDICAGO SATIVA;

EID: 0035119588     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/85029     Document Type: Article

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