Identification and characterisation of the Volvox carteri Moco carrier protein.
Molybdenum cofactor
prosthetic group insertion
prosthetic group transfer
Journal
Bioscience reports
ISSN: 1573-4935
Titre abrégé: Biosci Rep
Pays: England
ID NLM: 8102797
Informations de publication
Date de publication:
27 11 2020
27 11 2020
Historique:
received:
26
06
2020
revised:
08
10
2020
accepted:
13
10
2020
pubmed:
22
10
2020
medline:
13
4
2021
entrez:
21
10
2020
Statut:
ppublish
Résumé
The molybdenum cofactor (Moco) is a redox active prosthetic group found in the active site of Moco-dependent enzymes (Mo-enzymes). As Moco and its intermediates are highly sensitive towards oxidative damage, these are believed to be permanently protein bound during synthesis and upon maturation. As a major component of the plant Moco transfer and storage system, proteins have been identified that are capable of Moco binding and release but do not possess Moco-dependent enzymatic activities. The first protein found to possess these properties was the Moco carrier protein (MCP) from the green alga Chlamydomonas reinhardtii. Here, we describe the identification and biochemical characterisation of the Volvox carteri (V. carteri) MCP and, for the first time, employ a comparative analysis to elucidate the principles behind MCP Moco binding. Doing so identified a sequence region of low homology amongst the existing MCPs, which we showed to be essential for Moco binding to V. carteri MCP.
Identifiants
pubmed: 33084886
pii: 226728
doi: 10.1042/BSR20202351
pmc: PMC7687042
pii:
doi:
Substances chimiques
Carrier Proteins
0
Coenzymes
0
Metalloproteins
0
Molybdenum Cofactors
0
Plant Proteins
0
Pteridines
0
molybdenum cofactor
ATN6EG42UQ
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2020 The Author(s).
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