Disease relevance of svr

• Individual domains of Drosophila CPD were expressed in insect Sf9 cells using the baculovirus expression system [1].

High impact information on svr

• The structure revealed a tetrahedrally coordinated zinc ion that appears to be structurally analogous to the zinc coordination sites of zinc hydrolases, such as thermolysin and carboxypeptidase A. This previously unsuspected catalytic site represents a distinct activity from the autoprocessing activity that resides in the carboxy-terminal domain [2].
• Reduced presence of thylakoid membranes and loss of grana are found in the plastids of chlorotic leaves, indicating that antisense or sense AKR has blocked chloroplast differentiation [3].
• The chlorotic phenotype was genetically transmitted to the next generation, although most chlorotic plants produced much less seed [3].
• Gut-specific transcriptional regulatory elements of the carboxypeptidase gene are conserved between black flies and Drosophila [4].
• Here we characterize the putative promoter region of a black fly midgut carboxypeptidase gene and show that these sequences correctly direct the expression of a beta-glucuronidase reporter in Drosophila melanogaster [4].

Biological context of svr

• In addition, two alternative exons were found, which result in proteins with different carboxypeptidase-like domains, termed domains 1A and 1B [1].
• A variety of bioinformatics and experimental approaches were used to determine that the Drosophila silver gene corresponds to a CPD-like protein with three carboxypeptidase-like domains, a transmembrane domain, and a cytosolic tail [1].
• The differences in pH optima and substrate specificity between Drosophila domains 1B and 2 are similar to the differences between duck CPD domains 1 and 2, suggesting that these properties are essential to CPD function [1].
• PCR primers derived from two functional domains of vertebrate carboxypeptidase E (CPE) were used to generate a probe for screening a size-selected Drosophila melanogaster genomic library [5].
• This gut-specific black fly carboxypeptidase promoter provides a valuable tool for the study of disease vectors [4].

Anatomical context of svr

• At the nonpermissive temperature, processing of alkaline phosphatase and carboxypeptidase Y in arl3 mutant was slowed. yARL3 might be required for protein transport from endoplasmic reticulum to Golgi or from Golgi to vacuole at nonpermissive temperatures [6].
• Atonal regulates DE-cadherin transcriptionally, whereas the EGFR pathway, acting through the transcription factor Pointed, exerts its effects on adherens junctions indirectly, at a post-transcriptional level [7].
• When compared to the recently solved structures of the testis isoform of ACE (tACE) and its Drosophila homologue (AnCE), carboxypeptidase A showed little structural homology outside of the active site, while thermolysin revealed significant but less marked overall similarity [8].
• To investigate the role of the two different C-terminal tail sequences (tail-1 and tail-2) that result from the differential splicing within exon 8, constructs containing a reporter protein (albumin) attached to the transmembrane domain and tail-1 or tail-2 of CPD were expressed in S2 cells and a mouse pituitary cell line (AtT20 cells) [9].
• Vitellogenic carboxypeptidase is a 53 kDa yolk protein produced by the fat body of the female mosquito, Aedes aegypti, in response to a blood meal [10].

Associations of svr with chemical compounds

• This partial sequence, homologous to human CPE, CPM, and CPN, contained the conserved arginine and zinc binding domains [5].
• Using [Leu(5)]enkephalin as a substrate, a captopril sensitive dipeptidyl carboxypeptidase (angiotensin I-converting enzyme) and an amastatin-sensitive aminopeptidase were detected as prominent activities associated with intact discs [11].
• Characterization of a digestive carboxypeptidase from the insect pest corn earworm (Helicoverpa armigera) with novel specificity towards C-terminal glutamate residues [12].
• Activated HaCA42 carboxypeptidase hydrolysed a synthetic substrate for glutamate carboxypeptidases (FAEE, C-terminal Glu), but did not hydrolyse substrates for carboxypeptidase A or B (FAPP or FAAK, C-terminal Phe or Lys) or methotrexate, cleaved by clan MH glutamate carboxypeptidases [12].
• Male accessory gland secretory proteins in seven members of Drosophila nasuta subgroup were analyzed by SDS-PAGE in combination with different staining techniques such as CBB-R250, Silver, PAS, PAS-silver and zinc-imidazole reverse staining [13].

Other interactions of svr

• A search for other dHDAC3-like genes failed to find other potential paralogues in D. melanogaster, but identified significant homologies with bacterial and fungal genes encoding enzymes that metabolise acetyl groups, and with genes for other hydrolyases such as carboxypeptidase [14].

Analytical, diagnostic and therapeutic context of svr

• Molecular cloning of a Drosophila melanogaster gene coding for an homologue of human carboxypeptidase E [5].
• This peptide was shown to be the carboxyl terminus by sequence determination and by carboxypeptidase A digestion of the native protein [15].
• Carboxypeptidases were purified from guts of larvae of corn earworm (Helicoverpa armigera), a lepidopteran crop pest, by affinity chromatography on immobilized potato carboxypeptidase inhibitor, and characterized by N-terminal sequencing [12].

References