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

Zach Adam; Hanan Itzhaki; Amihud Borochov; Shimon Mayak

doi:10.1016/0168-9452(85)90147-5

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

Institute of Plant Sciences and Genetics in Agriculture

Research output: Contribution to journal › Article › peer-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 K_m of 4.1 mM for ACC, and possesses at least two catalytic subunits.

Original language	English
Pages (from-to)	89-93
Number of pages	5
Journal	Plant Science
Volume	42
Issue number	2
DOIs	https://doi.org/10.1016/0168-9452(85)90147-5
State	Published - 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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10.1016/0168-9452(85)90147-5

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title = "Substrate stimulation of an enzyme converting 1-aminocyclopropane-1-carboxylic acid to ethylene",

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.",

keywords = "1-aminocyclopropane-1-carboxylic acid, ethylene, ethylene-forming-enzyme",

author = "Zach Adam and Hanan Itzhaki and Amihud Borochov and Shimon Mayak",

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

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doi = "10.1016/0168-9452(85)90147-5",

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AU - Adam, Zach

AU - Itzhaki, Hanan

AU - Borochov, Amihud

AU - Mayak, Shimon

N1 - Funding Information: This project was supported by S.A. Schon-brunn research endowment fund of The Hebrew University of Jerusalem.

PY - 1985/12/19

Y1 - 1985/12/19

N2 - 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.

AB - 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.

KW - 1-aminocyclopropane-1-carboxylic acid

KW - ethylene

KW - ethylene-forming-enzyme

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VL - 42

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JO - Plant Science

JF - Plant Science

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ER -

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

Abstract

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Keywords

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