ArticleScientific reports2015
Structural basis of Ac-SDKP hydrolysis by Angiotensin-I converting enzyme.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- Structure-function insights into the digestive fate of angiotensin-converting enzyme-inhibitory peptides from microwave-treated corn gluten meal.Food chemistry. Molecular sciences · 2026Article
- Molecular basis of domain-specific angiotensin I-converting enzyme inhibition by the antihypertensive drugs enalaprilat, ramiprilat, trandolaprilat, quinaprilat and perindoprilat.The FEBS journal · 2026Article
- Molecular Basis of Dipeptide Recognition inBiomolecules · 2025Article
- Molecular basis of human angiotensin-1 converting enzyme inhibition by a series of diprolyl-derived compounds.The FEBS journal · 2025Article
- Advances in the structural basis for angiotensin-1 converting enzyme (ACE) inhibitors.Bioscience reports · 2024Review
- Aprotinin (I): Understanding the Role of Host Proteases in COVID-19 and the Importance of Pharmacologically Regulating Their Function.International journal of molecular sciences · 2024Review
- The potential role of renin angiotensin system in acute leukemia: a narrative review.Molecular biology reports · 2024Review
- Knockout of ACE-N facilitates improved cardiac function after myocardial infarction.Journal of molecular and cellular cardiology plus · 2023Article
- Impact of Gastrointestinal Digestion Simulation on the Formation of Angiotensin-I-Converting Enzyme Inhibitory (ACE-I) Peptides from Germinated Lamtoro Gung Flour.Foods (Basel, Switzerland) · 2022Article
- Structural basis for the inhibition of human angiotensin-1 converting enzyme by fosinoprilat.The FEBS journal · 2022Article
- Cryo-EM reveals mechanisms of angiotensin I-converting enzyme allostery and dimerization.The EMBO journal · 2022Article
- Evaluation of Biological Activity of Natural Compounds: Current Trends and Methods.Molecules (Basel, Switzerland) · 2022Review
- ACE2 and ACE: structure-based insights into mechanism, regulation and receptor recognition by SARS-CoV.Clinical science (London, England : 1979) · 2020Review
- Synthesis and Identification of a Novel Peptide, Ac-SDK (Biotin) Proline, That Can Elicit Anti-Fibrosis Effects in Rats Suffering from Silicosis.Drug design, development and therapy · 2020Article
- Interacting cogs in the machinery of the renin angiotensin system.Biophysical reviews · 2019Review
- Influence of the interaction between Ac‑SDKP and Ang II on the pathogenesis and development of silicotic fibrosis.Molecular medicine reports · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Angiotensin-I converting enzyme (ACE) is a zinc dipeptidylcarboxypeptidase with two active domains and plays a key role in the regulation of blood pressure and electrolyte homeostasis, making it the principal target in the treatment of cardiovascular disease. More recently, the tetrapetide N-acetyl-Ser-Asp-Lys-Pro (Ac-SDKP) has emerged as a potent antifibrotic agent and negative regulator of haematopoietic stem cell differentiation which is processed exclusively by ACE. Here we provide a detailed biochemical and structural basis for the domain preference of Ac-SDKP. The high resolution crystal structures of N-domain ACE in complex with the dipeptide products of Ac-SDKP cleavage were obtained and offered a template to model the mechanism of substrate recognition of the enzyme. A comprehensive kinetic study of Ac-SDKP and domain co-operation was performed and indicated domain interactions affecting processing of the tetrapeptide substrate. Our results further illustrate the molecular basis for N-domain selectivity and should help design novel ACE inhibitors and Ac-SDKP analogues that could be used in the treatment of fibrosis disorders.
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