Isopentenyl pyrophosphate isomerase:dimethylallyl pyrophosphate isomerase: isolation from Claviceps sp. SD 58 and comparison to the mammalian enzyme.
Arch Biochem Biophys
; 248(2): 620-5, 1986 Aug 01.
Article
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| MEDLINE
| ID: mdl-3740842
ABSTRACT
Isopentenyl pyrophosphate isomerasedimethyl pyrophosphate isomerase (EC 5.3.3.2) has been purified to near homogeneity from Claviceps sp. A molecular weight of 35,000 was found by gel exclusion chromatography as well as by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This indicates that the enzyme consists of a single subunit and is in contrast to the Mr 22,000 that we have found for the enzyme from liver. The lability of isomerase from liver, often reported, has been found to be due to its susceptibility to proteolysis. Nine compounds have been tested as inhibitors of both isomerases. The binding of analogs requires the pyrophosphate moiety which may be substituted by a variety of alkyl groups. Inclusion of a polar function in the hydrocarbon portion of the analog greatly reduces interaction with the enzyme. Reversibility of the reaction was not found with a higher homolog of the substrate.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Isomerasas de Doble Vínculo Carbono-Carbono
/
Isomerasas
Límite:
Animals
Idioma:
En
Revista:
Arch Biochem Biophys
Año:
1986
Tipo del documento:
Article