Substrate stimulation of an enzyme converting 1-aminocyclopropane-1-carboxylic acid to ethylene

Zach Adam*, Hanan Itzhaki, Amihud Borochov, Shimon Mayak

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The rate of conversion of 1-aminocyclopropane-1-carboxylic acid (ACC) to ethylene, catalyzed by a solubilized membrane fraction, gradually increases with time up to a factor of 5 at 120 min. The effects of the substrate and the products of this reaction on the reaction rate were tested. Preincubation of the solubilized enzyme with ethylene had no effect on the reaction rate, while CO2 increased it by 40% and CN- inhibited it by 65%. Pre-incubation of the enzyme with ACC significantly increased the reaction rate, in a manner resembling the observed time-dependent increase. Examination of the substrate-dependent activity over a wide range of concentrations reveals a sigmoidal curve. Analysis of the data by means of a Hill plot suggests that the enzyme converting ACC to ethylene has a Km of 4.1 mM for ACC, and possesses at least two catalytic subunits.

Original languageAmerican English
Pages (from-to)89-93
Number of pages5
JournalPlant Science
Volume42
Issue number2
DOIs
StatePublished - 19 Dec 1985

Bibliographical note

Funding Information:
This project was supported by S.A. Schon-brunn research endowment fund of The Hebrew University of Jerusalem.

Keywords

  • 1-aminocyclopropane-1-carboxylic acid
  • ethylene
  • ethylene-forming-enzyme

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