Crystal Structure of the Catalytic and Cytochrome
Agaricales
/ enzymology
Amino Acid Sequence
Bacteria
/ enzymology
Binding Sites
Carbohydrate Dehydrogenases
/ metabolism
Catalysis
Cytochromes b
/ chemistry
Electron Transport
Eukaryota
/ enzymology
Fungal Proteins
/ genetics
Fungi
/ enzymology
Glucose Dehydrogenases
/ metabolism
Models, Molecular
Oxidation-Reduction
Oxidoreductases
/ chemistry
PQQ Cofactor
/ chemistry
Protein Conformation
Protein Domains
X-Ray Diffraction
AA12
AA8
Carbohydrate-Active Enzymes database
Coprinopsis cinerea
cytochrome b
pyrroloquinoline quinone
Journal
Applied and environmental microbiology
ISSN: 1098-5336
Titre abrégé: Appl Environ Microbiol
Pays: United States
ID NLM: 7605801
Informations de publication
Date de publication:
15 12 2019
15 12 2019
Historique:
received:
24
07
2019
accepted:
10
09
2019
pubmed:
13
10
2019
medline:
22
8
2020
entrez:
13
10
2019
Statut:
epublish
Résumé
Pyrroloquinoline quinone (PQQ) was discovered as a redox cofactor of prokaryotic glucose dehydrogenases in the 1960s, and subsequent studies have demonstrated its importance not only in bacterial systems but also in higher organisms. We have previously reported a novel eukaryotic quinohemoprotein that exhibited PQQ-dependent catalytic activity in a eukaryote. The enzyme, pyranose dehydrogenase (PDH), from the filamentous fungus
Identifiants
pubmed: 31604769
pii: AEM.01692-19
doi: 10.1128/AEM.01692-19
pmc: PMC6881789
pii:
doi:
Substances chimiques
Fungal Proteins
0
PQQ Cofactor
72909-34-3
Cytochromes b
9035-37-4
Oxidoreductases
EC 1.-
Carbohydrate Dehydrogenases
EC 1.1.-
Glucose Dehydrogenases
EC 1.1.1.-
glucose dehydrogenase (pyrroloquinoline-quinone)
EC 1.1.5.2
cellobiose-quinone oxidoreductase
EC 1.1.99.18
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2019 Takeda et al.
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