EC Number   |
General Information |
Reference |
|---|
   4.4.1.14 | evolution |
the enzyme belongs to type-1 subfamily of plant 1-aminocyclopropane-1-carboxylate synthases |
730364 |
| 4.4.1.14 | metabolism |
1-aminocyclopropane-1-carboxylate synthase and 1-aminocyclopropane-1-carboxylate oxidase are key enzymes in the ethylene production |
729833 |
| 4.4.1.14 | metabolism |
abscisic acid, auxin, gibberellic acid, methyl jasmonic acid, and salicylic acid differentially regulate the stability of ACS proteins, with distinct effects on various isoforms. Heterodimerization between ACS isoforms from distinct subclades results in increased stability of the shorter-lived partner, i.e. isoform ACS7 has a regulatory function to influence the stability of type-1 and type-2 ACS proteins through the formation of heterodimers |
748957 |
| 4.4.1.14 | metabolism |
harvest periods related to soluble solids contents content of Hayward kiwifruit significantly affect 1-aminocyclopropane-1-carboxylate synthase activity, total soluble protein content and protein profile. ACC synthase activity is suppressed, especially in early harvested fruits, by an inhibition of fruit ripening during controlled atmosphere storage |
715189 |
| 4.4.1.14 | metabolism |
phosphorylation/dephosphorylation of ACS2 regulates its turnover upstream of the ubiquitin-26S-proteasome degradation pathway. ACS2 is stabilized by phosphorylation and degraded after dephosphorylation. The amount of ACS2 affected by the protein kinase/phosphatase inhibitors significantly influences cellular ACS activity, 1-aminocyclopropane-1-carboxylic acid content, and ethylene production levels in tomato fruit tissue. Calcium-dependent protein kinase CDPK2, is one of the protein kinases that are able to phosphorylate ACS2 at residue S460. ACS2 is immediately phosphorylated after translation by CDPK and mitogen-activated protein kinase at different sites in response to wound signaling and almost all functional ACS2 molecules are phosphorylated in the cell. Phosphorylation at both sites is required for ACS2 stability |
716539 |
| 4.4.1.14 | metabolism |
proteolytic turnover of the ACS6 protein is retarded when protein phosphatase 2A activity is reduced. Protein phosphatase 2A and ACS6 proteins associate in seedlings and RCN1-containing protein phosphatase 2A complexes specifically dephosphorylate a C-terminal ACS6 phosphopeptide |
716667 |
| 4.4.1.14 | metabolism |
the enzyme catalyzes the generally rate-limiting step in the biosynthesis of the phytohormone ethylene. 14-3-3 proteins exhibit a regulatory function in the pathway by reducing the degradation of 1-aminocyclopropane-1-carboxylate synthase through components of a CULLIN-3 E3 ubiquitin ligase, i.e. ethylene-overproducer 1-like proteins or ETO1/EOLs, that target a subset of the 1-aminocyclopropane-1-carboxylate synthase proteins for rapid degradation by the 26S proteasome. 14-3-3 protein positively regulates type-2 ACS protein stability by both increasing the turnover of the ETO1/EOL BTB E3 ligases that target type-2 ACS proteins and by an ETO1/EOL-independent mechanism. 14-3-3 protein promotes the degradation of ETO1/EOLs, likely via the 26S proteasome pathway |
730603 |
| 4.4.1.14 | metabolism |
the enzyme is important in ethylene production |
730269 |
| 4.4.1.14 | more |
14-3-3 proteins interact with multiple 1-aminocyclopropane-1-carboxylate synthase isoforms in Arabidopsis thaliana, 14-3-3 likely acts on all three classes of enzyme proteins |
730603 |
| 4.4.1.14 | physiological function |
cotton ACS2 interacts with Ca2+-dependent protein kinase CPK1. Phosphorylated ACS2 shows significantly increased ACS activity, leading to elevated ethylene production |
713608 |
