Zinc-metalloproteases in insects: ACE and ECE.
Research on the angiotensin-converting enzyme (ACE) in insects has substantially advanced during the recent decade. The cloning of this enzyme in many insect species, the determination of the 3D-structure and several molecular and physiological studies have contributed to the characterization of insect ACE as we know it today: a functional enzyme with a putative role in reproduction, development and defense. The discovery of the endothelin-converting enzyme in insects occurred more recently and cloning of the corresponding cDNA has been carried out in only one insect species so far. However, activity studies and analysis of insect genomes indicate that this enzyme is also widely distributed among insect species. Making hypotheses about its putative function would be preliminary, but its wide tissue distribution suggests a major and diverse biological role.
Macours
Nathalie
N
Laboratory for Developmental Physiology, Genomics and Proteomics, Katholieke Universiteit Leuven, Naamsestraat 59, B-3000 Leuven, Belgium. nathalie.macours@bio.kuleuven.ac.be
Hens
Korneel
K
D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry* / Q000235:genetics* / Q000502:physiology; D000072396:Endothelin-Converting Enzymes; D016678:Genome; D007313:Insecta / Q000201:enzymology*; D008666:Metalloendopeptidases; D008958:Models, Molecular; D008969:Molecular Sequence Data; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry* / Q000235:genetics* / Q000502:physiology; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D015032:Zinc / Q000737:chemistry / Q000378:metabolism
D007703:Peptidyl-Dipeptidase A; D016282:Aspartic Acid Endopeptidases; D008666:Metalloendopeptidases; D000072396:Endothelin-Converting Enzymes; D015032:Zinc