High impact information on Acer

• But disruption of ACER, a Drosophila ACE2 homologue, results in a severe defect of heart morphogenesis [1].
• These phosphinic peptides were potent inhibitors of Acer, but not of Ance [2].
• We conclude that the active sites of the N-domain and of Acer share structural features that permit the binding of the unusual RXP407 inhibitor and the hydrolysis of a broader range of peptide structures [2].
• Acer mRNA is found in the developing dorsal vessel (heart) during embryogenesis [3].
• Only two of the peptides, [Leu(5)]enkephalinamide and leucokinin-I were cleaved faster by Acer [4].

Biological context of Acer

• Peptidyl dipeptidases (Ance and Acer) of Drosophila melanogaster: major differences in the substrate specificity of two homologs of human angiotensin I-converting enzyme [4].
• Furthermore, Acer did not hydrolyse the synthetic substrates Phe-Ser-Pro-Arg-Leu-Gly-Arg-Arg and Phe-Ser-Pro-Arg-Leu-Gly-Lys-Arg, two partially processed putative locustamyotropin precursors, under conditions where Ance produced 82% substrate hydrolysis [5].
• One of these (Acer) is expressed in the embryonic heart, whereas the second enzyme (Ance) is expressed in several tissues at different stages of the life cycle [6].
• The predicted open reading frame encoded 648 amino acids with about 50% identities with the Drosophila melanogaster angiotensin-converting enzyme Ance and Acer [7].
• We isolated a clone encoding a putative angiotensin-converting enzyme-related gene from the wing disc cDNA library of the silkworm, Bombyx mori (refer to as BmAcer) [7].

Associations of Acer with chemical compounds

• The Drosophila melanogaster-related angiotensin-I-converting enzymes Acer and Ance--distinct enzymic characteristics and alternative expression during pupal development [5].
• Acer was inhibited by captopril, trandolaprilat and enalaprilat, with apparent Ki values in the nanomolar range, whereas lisinopril and fosinoprilat were less potent [5].
• The replacement of Asp360 with a histidine in ACER would explain the higher K(m) recorded for the hydrolysis of BK peptides by this enzyme [8].

Other interactions of Acer

• Ance was generally much better than Acer at hydrolyzing peptides of 5-13 amino acids in length [4].

Analytical, diagnostic and therapeutic context of Acer

• We have investigated the relationship of Ance and Acer to the N- and C-domains of human sACE by genomic sequence analysis and by using domain-selective inhibitors, including RXP 407, a selective inhibitor of the human N-domain [2].

References