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. 1975 Feb;55(2):377–381. doi: 10.1104/pp.55.2.377

Substrate Specificity of Chlorophyllase 1,2

Roger F McFeeters a
PMCID: PMC541619  PMID: 16659086

Abstract

Apparent Km and Vmax values were obtained for hydrolysis of methyl and ethyl chlorophyllides a, methyl and ethyl pheophorbide a, and 9-hydroxymethyl pheophorbide a by chlorophyllase from Ailanthus altissima. Analysis of substrate specificity data for chlorophyllase indicates that the presence of a 9-keto group and a methyl alcohol group esterified at the 7-position in chlorophyll derivatives results in maximum binding affinity for substrates. Data on maximum reaction rates indicate that the rate-controlling step of hydrolysis occurs after release of the alcohol from the ester. Probable high affinity chlorophyllase inhibitors can be predicted on the basis of these specificity studies.

An improved method for purification of chlorophyllase has been developed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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