Influence of tryptic hydrolysis on the enzymatic function of the membrane-bound form of particulate methane monooxygenase from Methylosinus trichosporium OB3b.
C-terminal region
Particulate methane monooxygenase
Selective proteolysis
Stability in vitro
Trypsin digestion
Journal
Journal of biotechnology
ISSN: 1873-4863
Titre abrégé: J Biotechnol
Pays: Netherlands
ID NLM: 8411927
Informations de publication
Date de publication:
10 Nov 2020
10 Nov 2020
Historique:
received:
03
04
2020
revised:
30
07
2020
accepted:
17
08
2020
pubmed:
24
8
2020
medline:
27
8
2021
entrez:
24
8
2020
Statut:
ppublish
Résumé
Particulate methane monooxygenase (pMMO) is a membrane protein embedded in the intracytoplasmic membrane of methane-oxidizing bacteria. Structural analysis of pMMO showed the existence of a hydrophilic region exposed outside of the bacterial membrane. To obtain information regarding the role of this hydrophilic region in the enzymatic function of pMMO, trypsin proteolysis of the membrane-bound form of pMMO from Methylosinus trichosporium OB3b was performed at 4 °C. The polypeptides produced by this hydrolysis were analyzed by polyacrylamide gel electrophoresis and MALDI-TOF/TOF. Furthermore, the influence of this tryptic digestion on the methane hydroxylation and propene epoxidation enzymatic activities of pMMO was investigated. Among the three subunits of pMMO, PmoB and PmoC were hydrolyzed by trypsin, but PmoA was not. With 10 mg L
Identifiants
pubmed: 32828830
pii: S0168-1656(20)30219-4
doi: 10.1016/j.jbiotec.2020.08.006
pii:
doi:
Substances chimiques
Alkenes
0
Epoxy Compounds
0
Membrane Proteins
0
Copper
789U1901C5
propylene
AUG1H506LY
Oxygenases
EC 1.13.-
methane monooxygenase
EC 1.14.13.25
Trypsin
EC 3.4.21.4
propylene oxide
Y4Y7NYD4BK
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
98-106Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.