Title: Purification of isopentenyl pyrophosphate isomerase and geranylgeranyl pyrophosphate synthase from Capsicum chromoplasts by affinity chromatography
Abstract: A procedure based on affinity chromatography was used for the purification to homogeneity of isopentenyl pyrophosphate isomerase and geranylgeranyl pyrophosphate synthase from Capsicum chromoplasts. Isopentenyl pyrophosphate isomerase is a monomeric protein and has a molecular weight of 33 500 ± 500. The Michaelis constant for isopentenyl pyrophosphate was 6 μM. Geranylgeranyl pyrophosphate synthase has a native molecular weight of 74 000 ± 2000 resulting from the association of two apparently identical subunits having a molecular weight of 37000 ± 1000. The dimeric structure of geranylgeranyl pyrophosphate synthase was confirmed using a photolabile analog of geranyl pyrophosphate (2-diazo-3-trifluoropropionyloxygeranyl pyrophosphate). Geranylgeranyl pyrophosphate synthase catalyzed the prenyl transfer reaction isopentenyl pyrophosphate (Km = 3 μM) and either dmiethylallyl pyrophosphate (Km = 0.95 μM), pyrophosphate (Km = 1 μM) or farnesyl pyrophosphate (Km = 1.2 μM) as aliylic partners. The three prenyl transfer reactions were inhibited when the enzyme was irradiated with the photolabile analog of geranyl pyrophosphate.
Publication Year: 1987
Publication Date: 1987-07-01
Language: en
Type: article
Indexed In: ['crossref']
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Cited By Count: 115
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