ArticleGene2007
Characterization of the first angiotensin-converting like enzyme in bacteria: Ancestor ACE is already active.
Article in Gene, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 32 citations in OpenAlex.
- Fecal ACE and ACE2 Activities Reflect Intestinal Shedding and Microbiota Modulation of Renin-Angiotensin System.Biology · 2026Article
- Article
- An update on angiotensin-converting enzyme 2 structure/functions, polymorphism, and duplicitous nature in the pathophysiology of coronavirus disease 2019: Implications for vascular and coagulation disease associated with severe acute respiratory syndrome coronavirus infection.Frontiers in microbiology · 2022Review
- Gut microbiota and renin-angiotensin system: a complex interplay at local and systemic levels.American journal of physiology. Gastrointestinal and liver physiology · 2021Review
- Genetic changes involving the coral gastrovascular system support the transition between colonies and bailed-out polyps: evidence from a Pocillopora acuta transcriptome.BMC genomics · 2021Article
- Review
- TheMicroorganisms · 2021Article
- Altitudinal variation of the gut microbiota in wild house mice.Molecular ecology · 2019Article
- Review
- Interkingdom pharmacology of Angiotensin-I converting enzyme inhibitor phosphonates produced by actinomycetes.ACS medicinal chemistry letters · 2014Article
- Will the real angiotensin converting enzyme please stand up?Journal of molecular medicine (Berlin, Germany) · 2012Article
- Emergence and evolution of the renin-angiotensin-aldosterone system.Journal of molecular medicine (Berlin, Germany) · 2012Review
- Angiotensin-converting enzyme is required for normal myelopoiesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
- A crucial role in fertility for the oyster angiotensin-converting enzyme orthologue CgACE.PloS one · 2011Article
- Not just angiotensinases: new roles for the angiotensin-converting enzymes.Cellular and molecular life sciences : CMLS · 2010Review
- New insights into the role of angiotensin-converting enzyme obtained from the analysis of genetically modified mice.Journal of molecular medicine (Berlin, Germany) · 2008Review
- Identification of ACE pharmacophore in the phosphonopeptide metabolite K-26.Bioorganic & medicinal chemistry letters · 2008Article
Corrections and comments
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Authors and funding
9 authors at 7 institutions in 3 countries.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.