Identification of an Additional Metal-Binding Site in Human Dipeptidyl Peptidase III.
binding affinity
dipeptidyl peptidase III
metal exchange
metal inhibition
metal ions
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
13 Aug 2023
13 Aug 2023
Historique:
received:
12
07
2023
revised:
03
08
2023
accepted:
11
08
2023
medline:
28
8
2023
pubmed:
26
8
2023
entrez:
26
8
2023
Statut:
epublish
Résumé
Dipeptidyl peptidase III (DPP III, EC 3.4.14.4) is a monozinc metalloexopeptidase that hydrolyzes dipeptides from the N-terminus of peptides consisting of three or more amino acids. Recently, DPP III has attracted great interest from scientists, and numerous studies have been conducted showing that it is involved in the regulation of various physiological processes. Since it is the only metalloenzyme among the dipeptidyl peptidases, we considered it important to study the process of binding and exchange of physiologically relevant metal dications in DPP III. Using fluorimetry, we measured the
Identifiants
pubmed: 37628928
pii: ijms241612747
doi: 10.3390/ijms241612747
pmc: PMC10454320
pii:
doi:
Substances chimiques
dipeptidyl peptidase III
EC 3.4.14.4
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
EC 3.4.14.-
DPP3 protein, human
EC 3.4.14.4
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Croatian Science Foundation
ID : IP-2018-01-2936
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