Characterization of the first angiotensin-converting like enzyme in bacteria: Ancestor ACE is already active
| Autor: | Guillaume Riviere, Jean-Pierre Bohin, K. Ravi Acharya, Edward D. Sturrock, Didier Vieau, Pierre Corvol, Hazel R. Corradi, Annie Michaud, Virginie Cogez |
|---|---|
| Přispěvatelé: | Unité Neurosciences et Physiologie Adaptative, Université de Lille, Sciences et Technologies, Pathologie vasculaire et endocrinologie rénale - Chaire de médecine expérimentale (INSERM U36), Collège de France (CdF (institution))-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Biology and Biochemistry, University of Bath [Bath], Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Pathologie vasculaire et endocrinologie rénale, Collège de France (CdF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université de Lille-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Mca
7-methoxycoumarin-4-yl)-diacetyl Protein Conformation DNase desoxyribonuclease Angiotensin-Converting Enzyme Inhibitors Biochemistry FPLC fast protein liquid chromatography bp base pair(s) ACE gene encoding ACE Cloning Molecular Peptide sequence Phylogeny DpaOH N3(2 4-dinitrophenyl)l-2 3-diaminopropionyl-OH HHL Hippuryl-Histidyl-Leucine chemistry.chemical_classification 0303 health sciences cDNA DNA complementary to RNA biology Angiotensin II 030302 biochemistry & molecular biology pv pathovar RNase: ribonuclease General Medicine enk-NH2 enkephalinamide enk enkephalin [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Xanthomonas axonopodis kDa kilodalton DMSO dimethylsulfoxide SDS sodium dodecyl sulfate rXcACE recombinant Xanthomonas axonopodis pv citri Angiotensin-converting enzyme Evolution In silico Molecular Sequence Data Conservation Peptidyl-Dipeptidase A Article CHO chinese hamster ovary kb kilobase(s) Structure-Activity Relationship 03 medical and health sciences ORF open reading frame Xc Xanthomonas axonopodis pathovar citri Bacterial Proteins Complementary DNA Genetics Amino Acid Sequence C- carboxy ng nanogram(s) PAGE polyacrylamide gel electrophoresis Ac acetyl 030304 developmental biology Sequence Homology Amino Acid Structure Computational Biology Active site ACE Angiotensin-converting enzyme dNTP deoxyribonucleoside triphosphate Carboxypeptidase Protease Open reading frame Enzyme nXcACE native Xanthomonas axonopodis pv citri Angiotensin-converting enzyme chemistry HPLC high-performance liquid chromatography biology.protein N- amino Angiotensin I Genome Bacterial Ang Angiotensin Cloning |
| Zdroj: | Gene Gene, Elsevier, 2007, 399 (1), pp.81-90. ⟨10.1016/j.gene.2007.05.010⟩ Gene, 2007, 399 (1), pp.81-90. ⟨10.1016/j.gene.2007.05.010⟩ |
| ISSN: | 0378-1119 1879-0038 |
| Popis: | International audience; Angiotensin-converting enzyme (ACE) is a metallopeptidase that converts angiotensin I into angiotensin II. ACE is crucial in the control of cardiovascular and renal homeostasis and fertility in mammals. In vertebrates, both transmembrane and soluble ACE, containing one or two active sites, have been characterized. So far, only soluble, single domain ACEs from invertebrates have been cloned, and these have been implicated in reproduction in insects. Furthermore, an ACE-related carboxypeptidase was recently characterized in Leishmania, a unicellular eukaryote, suggesting the existence of ACE in more distant organisms. Interestingly, in silico databank analysis revealed that bacterial DNA sequences could encode putative ACE-like proteins, strikingly similar to vertebrates' enzymes. To gain more insight into the bacterial enzymes, we cloned the putative ACE from the phytopathogenic bacterium, Xanthomonas axonopodis pv. citri, named XcACE. The 2 kb open reading frame encodes a 672-amino-acid soluble protein containing a single active site. In vitro expression and biochemical characterization revealed that XcACE is a functional 72 kDa dipeptidyl-carboxypeptidase. As in mammals, this metalloprotease hydrolyses angiotensin I into angiotensin II. XcACE is sensitive to ACE inhibitors and chloride ions concentration. Variations in the active site residues, highlighted by structural modelling, can account for the different substrate selectivity and inhibition profile compared to human ACE. XcACE characterization demonstrates that ACE is an ancestral enzyme, provoking questions about its appearance and structure/activity specialisation during the course of evolution. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect