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Dimethylallylpyrophosphate:3,9‐dihydroxypterocarpan 10‐dimethylallyl transferase from Phaseolus vulgaris Identification of the reaction product and properties of the enzyme
Author(s) -
Biggs David R.,
Welle Roland,
Visser Frans R.,
Grisebach Hans
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80909-2
Subject(s) - phaseolus , prenylation , chemistry , enzyme , microsome , elicitor , biochemistry , transferase , botany , biology
A microsomal fraction of elicitor‐challenged bean ( Phaseolus vulgaris ) cell suspension cultures catalyses the prenylation of 3,9‐dihydroxypterocarpan (DHP) to 3,9‐dihydroxy‐10‐dimethylallylpterocarpan (phaseollidin) with dimethylallylpyrophosphate (DMAPP) as the prenyl donor. K m values for DMAPP and DHP are in the range 1–3 μM. Strong product inhibition with phaseollidin and phaseollin is observed.