Dependence of in Vivo Ethylene Production Rate on 1-Aminocyclopropane-1-Carboxylic Acid Content and Oxygen Concentrations
Author(s) -
Wing-Kin Yip,
Xin-Zhi Jiao,
Shang Fa Yang
Publication year - 1988
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.88.3.553
Subject(s) - ethylene , 1 aminocyclopropane 1 carboxylic acid , chemistry , etiolation , malus , substrate (aquarium) , in vivo , oxygen , enzyme , biochemistry , horticulture , organic chemistry , biology , catalysis , ecology , microbiology and biotechnology
1-Aminocyclopropane-1-carboxylic acid (ACC) is aerobically oxidized in plant tissues to form ethylene by ethylene-forming enzyme (EFE). The effect of substrate (ACC and oxygen) concentrations on ethylene production rate by plant tissues was investigated. The K(m) value for O(2) in ethylene production varied greatly depending on the internal ACC content. When ACC levels in the tissue were low (below its K(m) value), the concentration of O(2) giving half-maximal ethylene production rate ([S](0.5)) ranged between 5 and 7%, and was similar among different tissues. As the concentration of ACC was increased (greater than its K(m) value), [S](0.5) for O(2) decreased markedly. In contrast, the K(m) value for ACC was not much dependent on O(2) concentration, but varied greatly among different plant tissues, ranging from 8 micromolar in apple (Malus sylvestris Mill.) tissue to 120 micromolar in etiolated wheat (Triticum aestivum) leaf. Such a great variation was thought to be due to the different compartmentation of ACC within the cells in different tissues. These kinetic data are consistent with the view that EFE follows an ordered binding mechanism in which EFE binds first to O(2) and then to ACC.
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