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Article

Kinetic and structural characterization of amyloid-β peptide hydrolysis by human angiotensin-1-converting enzyme.

The FEBS journal - 1 Mar 2016

Larmuth Kate M, Masuyer Geoffrey, Douglas Ross G, Schwager Sylva L, Acharya K Ravi, Sturrock Edward D

Abstract excerpt

UNLABELLED: Angiotensin-1-converting enzyme (ACE), a zinc metallopeptidase, consists of two homologous catalytic domains (N and C) with different substrate specificities. Here we report kinetic parameters of five different forms of human ACE with various amyloid beta (Aβ) substrates together with high resolution crystal structures of the N-domain in complex with Aβ fragments. For the physiological Aβ(1-16)...

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Share to Amyloid beta-Peptides
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrolysis

Share to In Vitro Techniques

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Share to Peptidyl-Dipeptidase A

Share to Protein Interaction Domains and Motifs

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Source

Open in PubMed Open full text

Identifiers

PMID: 26748546
DOI: 10.1111/febs.13647
PMCID: PMC4950319

Genes

ACE

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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