Different roles of the diphosphate moieties of allylic and homoallylic diphosphates in prenyltransferase reaction

Biochemical and Biophysical Research Communications

Volumn 156, Issue 1, 1988, Pages 396-402

  Gotoh, Takeshi ^a   Koyama, Tanetoshi ^a   Ogura, Kyozo ^a  

^a TOHOKU UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BISPHOSPHONIC ACID DERIVATIVE; DIMETHYLALLYLTRANSFERASE; ISOPENTENYL METHYLENEDIPHOSPHONATE; TRANSFERASE;

ANIMAL; ARTICLE; BINDING SITE; ENZYME SPECIFICITY; ENZYMOLOGY; KINETICS; LIVER; METABOLISM; PROTEIN BINDING; SWINE; SYNTHESIS;

ANIMAL; BINDING SITES; DIMETHYLALLYLTRANSTRANSFERASE; DIPHOSPHONATES; KINETICS; LIVER; PROTEIN BINDING; SUBSTRATE SPECIFICITY; SUPPORT, NON-U.S. GOV'T; SWINE; TRANSFERASES;

EID: 0024286279     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/S0006-291X(88)80854-4     Document Type: Article

References (8)

1. The significance of the diphosphate linkage involved in the substrates for prenyltransferase. Geranyl- and dimethylallyl methylenediphosphonate as artificial substrates.