High impact information on PHACS

• Expression of antisense RNA to the rate-limiting enzyme in the biosynthetic pathway of ethylene, 1-aminocyclopropane-1-carboxylate synthase, inhibits fruit ripening in tomato plants [1].
• A 17-kilobase (kb) region of the zucchini (Cucurbita pepo) genome has been sequenced and contains two genes, CP-ACC1A and CP-ACC1B, encoding 1-aminocyclopropane-1-carboxylate synthase (ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase, EC 4.4.1.14) [2].
• Characterization and sequencing of the active site of 1-aminocyclopropane-1-carboxylate synthase [3].
• Differential expression of 1-aminocyclopropane-1-carboxylate synthase genes during orchid flower senescence induced by the protein phosphatase inhibitor okadaic acid [4].
• Nucleotide sequence of a cDNA for 1-aminocyclopropane-1-carboxylate synthase from melon fruits [5].

Biological context of PHACS

• Molecular modeling data illustrate that the conservation of residues between PHACS and the plant ACSs is dispersed throughout its structure and that two active site residues that are important for ACS activity in plants are not conserved in PHACS [6].
• PHACS does, however, catalyze the deamination of L-vinylglycine, a known side-reaction of apple ACS [6].
• Identification of two new members of the 1-aminocyclopropane-1-carboxylate synthase-encoding multigene family in mung bean [7].
• The Female-Specific Cs-ACS1G Gene of Cucumber. A Case of Gene Duplication and Recombination between the Non-Sex-Specific 1-Aminocyclopropane-1-Carboxylate Synthase Gene and a Branched-Chain Amino Acid Transaminase Gene [8].
• RFLP analysis of 1-aminocyclopropane-1-carboxylate synthase ACC2 and ACC4 genes from Polish cultivars of tomato [9].

Associations of PHACS with chemical compounds

• Purified recombinant PHACS, expressed in Pichia pastoris, contains bound pyridoxal-5'-phosphate (PLP), but does not catalyze the synthesis of ACC [6].
• Here we show that calyculin A, a potent inhibitor of protein phosphatases, mimics the action of elicitors and, at nanomolar concentrations, induces medium alkalinization as well as a strong increase in the activity of 1-aminocyclopropane-1-carboxylate synthase, the key enzyme of ethylene biosynthesis [10].
• Crystals of recombinant 1-aminocyclopropane-1-carboxylate synthase from apple have been obtained with polyethylene glycol as precipitant using a combination of vapour diffusion and macroseeding techniques [11].
• Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues [12].
• Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant [13].

Analytical, diagnostic and therapeutic context of PHACS

• Crystallization and preliminary X-ray analysis of recombinant 1-aminocyclopropane-1-carboxylate synthase from apple. A key enzyme in the biosynthesis of the plant hormone ethylene [11].
• Molecular cloning of an 1-aminocyclopropane-1-carboxylate synthase from senescing carnation flower petals [14].
• Two-dimensional gel electrophoresis indicates that 1-aminocyclopropane-1-carboxylate synthase activity is associated with a 45-kDa polypeptide, with a pI of 5.8 +/- 0 [15].
• 1-Aminocyclopropane-1-carboxylate synthase was purified 5000-fold from LiCl-induced tomato fruit slices by conventional and high-performance liquid chromatography [15].

References