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Titolo:
MOLECULAR-CLONING AND CHARACTERIZATION OF OSYL-L-METHIONINE-SCOULERINE-9-O-METHYLTRANSFERASE FROM CULTURED-CELLS OF COPTIS-JAPONICA
Autore:
TAKESHITA N; FUJIWARA H; MIMURA H; FITCHEN JH; YAMADA Y; SATO F;
Indirizzi:
KYOTO UNIV,FAC AGR,DEPT AGR CHEM,SAKYO KU KYOTO 60601 JAPAN KYOTO UNIV,FAC AGR,DEPT AGR CHEM,SAKYO KU KYOTO 60601 JAPAN
Titolo Testata:
Plant and Cell Physiology
fascicolo: 1, volume: 36, anno: 1995,
pagine: 29 - 36
SICI:
0032-0781(1995)36:1<29:MACOO>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADENOSYL-L-METHIONINE; O-METHYLTRANSFERASE; NUCLEOTIDE-SEQUENCE; FORMING ENZYME; EXPRESSION; BERBERINE; BIOSYNTHESIS; PURIFICATION; TRANSFERASE; PATHWAY;
Keywords:
BERBERINE BIOSYNTHESIS; CDNA CLONING; COPTIS JAPONICA; HETEROLOGOUS EXPRESSION IN ESCHERICHIA-COLI; RANUNCULACEAE OSYL-L-METHIONINE-SCOULERINE-9-O-METHYLTRANSFERASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
N. Takeshita et al., "MOLECULAR-CLONING AND CHARACTERIZATION OF OSYL-L-METHIONINE-SCOULERINE-9-O-METHYLTRANSFERASE FROM CULTURED-CELLS OF COPTIS-JAPONICA", Plant and Cell Physiology, 36(1), 1995, pp. 29-36

Abstract

S-Adenosyl-L-methionine : scoulerine-9-O-methyltransferase (SMT) catalyzes the transfer of the S-methyl group of S-adenosyI-L-methionine tothe 9-hydroxyl group of scoulerine during the biosynthesis of berberine. We have isolated functionally active cDNA clones (pCJSMTs) from a cDNA library prepared from cultured cells of Coptis japonica. The longest cDNA insert (pCJSMT1) had an open reading frame that encoded 351 amino acids, but the calculated molecular mass (38,364 Da) of the deduced product was slightly lower than the experimentally determined molecular mass of purified SMT. Rapid amplification of the 5' end of the cDNA indicated that the full-length cDNA of SMT consisted of 1,458 nucleotides that encoded 381 amino acids. When the full-length cDNA was expressed in E. coli, the molecular mass of the expressed SMT was greaterthan that of native SMT in Coptis cells. This result suggests that SMT might be produced in a pre-mature form and processed post-translationally. SMT was also found to exhibit sequence homology to other O-methyltransferases from plants and N-terminal region of the SMT polypeptide appeared to be necessary for enzymatic activity.

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Documento generato il 04/04/20 alle ore 07:47:04