A comparative investigation of catalytic mechanism and domain between catechol-O-methyltransferase isoforms by isomeric shikonin and alkannin.
COMTs
Isomers
Ligand-receptor interaction
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
01 Jul 2023
01 Jul 2023
Historique:
received:
03
01
2023
revised:
12
04
2023
accepted:
02
05
2023
medline:
19
6
2023
pubmed:
8
5
2023
entrez:
7
5
2023
Statut:
ppublish
Résumé
The differences in catalytic mechanism and domain between the soluble (S-COMT) and membrane-bound catechol-O-methyltransferase (MB-COMT) are poorly documented due to the unavailable crystal structure of MB-COMT. Considering the enzymatic nature of S-COMT and MB-COMT, the challenge could be solvable by probing the interactions between the enzymes with the ligands with minor differences in structures. Herein, isomeric shikonin and alkannin bearing a R/S -OH group in side chain at the C2 position were used for domain profiling of COMTs. Human and rat liver-derived COMTs showed the differences in inhibitory response (human's IC
Identifiants
pubmed: 37150367
pii: S0141-8130(23)01652-5
doi: 10.1016/j.ijbiomac.2023.124758
pii:
doi:
Substances chimiques
shikonin
3IK6592UBW
Catechol O-Methyltransferase
EC 2.1.1.6
alkannin
075CRZ9995
Protein Isoforms
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
124758Informations de copyright
Copyright © 2023. Published by Elsevier B.V.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare no competing financial interest.