Abstract

The ethylene precursor, 1‐aminocyclopropane‐1‐carboxylic acid (ACC), is actively transported across the tonoplast of plant cells, impacting cellular compartmentation of ACC and ethylene biosynthesis. In the present study, the effects of ACC and amino acid analogs on ACC uptake into isolated maize (Zea mays L. cv. Golden Cross Bantam) mesophyll vacuoles were investigated to identify the stereospecific and structural features that are important in molecular recognition by the ACC transport system. Of the four stereoisomers of l‐amino‐2‐ethylcyclopropane‐l‐carboxylic acid (AEC), (1S, 2R)‐(–)‐AEC having a configuration corresponding to an L‐amino acid was the preferred substrate for the ACC transport system, competitively inhibiting ACC transport with a Ki of 18 μM. Of 11 neutral amino acid stereoisomers, L‐isomers were stronger inhibitors of ACC transport than corresponding D‐isomers. Neutral L‐amino acids with nonpolar side chains generally were more inhibitory than those with polar side chains, whereas several cationic and anionic L‐amino acids were ineffective antagonists of ACC transport. These observations suggest that the ACC transport system is stereospecific for relatively nonpolar, neutral L‐amino acids. This conclusion was supported by the observation that group additions, substitutions, or deletions at the carboxyl. α‐amino and the Pro‐ (R) methylene or hydrogen moieties (analogous to D‐amino acids) of ACC and other neutral amino acids and analogs essentially eliminated transport inhibition. In contrast, L‐amino acid analogs with variable substitutions at the distal end of the molecule remained antagonists. The relative activity of analogs was influenced by the length and degree of unsaturation of the side chain and by the location of side chain branching. Increasing the ring size of ACC analogs reduced antagonism whereas incorporating the α‐amino group into the ring structure as an L‐amino acid increased antagonism. The kinetics of L‐methoxyvinylglycine, L‐methionine. p‐nitro‐L‐phenylalanine and 1‐aminocyclobutane‐l‐carboxylic acid were competitive with Ki values of 3, 13, 16 and 19 μM, respectively. These results indicate that the ACC transport system can be classifie as a neutral L‐amino acid carrier having a relatively high affinity for ACC and other nonpolar amino acids. The results also suggest that the carrier interacts with the carboxyl, α‐amino and Pro‐(R) groups and with other less restricted side chain substituents of substrate amino acids.

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