The atypical binding mechanism of second calcium on phospholipase A2 group IIE.
Catalysis
Group IIE
Mutation
Phospholipase A2
Second calcium
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
11 06 2021
11 06 2021
Historique:
received:
31
03
2021
accepted:
09
04
2021
pubmed:
25
4
2021
medline:
10
8
2021
entrez:
24
4
2021
Statut:
ppublish
Résumé
Secreted phospholipase A2s (sPLA2s) are calcium dependent enzymes involved in various biological events such as lipid metabolism and inflammation. We previously identified the second calcium (Ca2) binding site of human sPLA2 Group IIE (hGIIE) by structural study and suggested that Asn21 act as the switch of Ca2 binding to modulate the enzymatic activity, but the detailed Ca2 binding mechanism is still unclear. Combined with enzymatic assay, model analysis and calcium binding affinity data for mutated hGIIE proteins, we herein further demonstrate that the flexibly bound Ca2 is essential for the catalysis of hGIIE, unlike the stable binding of Ca2 in hGIIA that replenishes the calcium in the typical loop during the reaction. The atypical Ca2 binding feature of hGIIE will provide a better understanding on the catalytic mechanism of hGIIE.
Identifiants
pubmed: 33894413
pii: S0006-291X(21)00633-1
doi: 10.1016/j.bbrc.2021.04.030
pii:
doi:
Substances chimiques
Recombinant Proteins
0
Group II Phospholipases A2
EC 3.1.1.4
Calcium
SY7Q814VUP
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
267-272Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no competing interests.