Partial purification and characterization of the short-chain prenyltransferases, gernayl diphospate synthase and farnesyl diphosphate synthase, from Abies grandis (grand fir).
Arch Biochem Biophys
; 386(2): 233-42, 2001 Feb 15.
Article
em En
| MEDLINE
| ID: mdl-11368347
ABSTRACT
In the conifer Abies grandis (grand fir), a secreted oleoresin rich in mono-, sesqui-, and diterpenes serves as a constitutive and induced defense against insects and pathogenic fungi. Geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) synthase, two enzymes which form the principal precursors of the oleoresin mono- and sesquiterpenes, were isolated from the stems of 2-year-old grand fir saplings. These enzymes were partially purified by sequential chromatography on DEAE-Sepharose, Mono-Q, and phenyl-Sepharose to remove competing phosphohydrolase and isopentenyl diphosphate (IPP) isomerase activities. GPP and FPP synthase formed GPP and E,E-FPP, respectively, as the sole products of the enzymatic condensation of IPP and dimethylallyl diphosphate (DMAPP). The properties of both enzymes are broadly similar to those of other prenyltransferases. The apparent native molecular masses are 54 +/- 3 kDa for GPP synthase and 110 +/- 6 kDa fo
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Alquil e Aril Transferases
/
Cycadopsida
Idioma:
En
Revista:
Arch Biochem Biophys
Ano de publicação:
2001
Tipo de documento:
Article
País de afiliação:
Alemanha