Affiliation:
1. Botanisches Institut, Universität München, Menziger Str. 67, D-8000 München 19
Abstract
Abstract
The esterification of various chlorophyllides with geranylgeranyl diphosphate was investigated as catalyzed by the enzyme chlorophyll synthetase. The enzyme source was an etioplast membrane fraction from etiolated oat seedlings (Avena sativa L.). The following chlorophyllides were prepared from the corresponding chlorophylls by the chlorophyllase reaction: chlorophyllide a (2) and b (4), bacteriochlorophyllide a (5), 3-acetyl-3-devinylchlorophyllide a (6), and pyrochlorophyllide a (7). The substrates were solubilized with cholate which reproducibly reduced the activity of chlorophyll synthetase by 40-50% . It was found that the following compounds were good substrates for chlorophyll synthetase: chlorophyllide a and b, 3-acetyl-3-devinylchloro-phyllide a, and pyrochlorophyllide a. Only a poor or no reaction was found with protochlorophyllide, pheophorbide a, and bacteriochlorophyllide. This difference of reactivity was not due to distribution differences of the substrates between solution and pelletable membrane fraction. Furthermore, no interference between good and poor substrate was detected. Structural features necessary for chlorophyll synthetase substrates were discussed.
Subject
General Biochemistry, Genetics and Molecular Biology
Cited by
38 articles.
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