Considerations Regarding Activity Determinants of Fungal Polyphenol Oxidases Based on Mutational and Structural Studies.
Thermothelomyces thermophila
X-ray structure
kinetic analysis
polyphenol oxidase
protein engineering
site-directed mutagenesis
tyrosinase
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:
11 05 2021
11 05 2021
Historique:
received:
25
02
2021
accepted:
16
03
2021
pubmed:
21
3
2021
medline:
2
6
2021
entrez:
20
3
2021
Statut:
epublish
Résumé
Polyphenol oxidases (PPOs) are an industrially relevant family of enzymes, being involved in the postharvest browning of fruits and vegetables, as well as in human melanogenesis. Their involvement lies in their ability to oxidize phenolic or polyphenolic compounds, which subsequently form pigments. The PPO family includes tyrosinases and catechol oxidases, which, in spite of their high structural similarity, exhibit different catalytic activities. Long-standing research efforts have not yet managed to decipher the structural determinants responsible for this differentiation, as every new theory is disproved by a more recent study. In the present work, we combined biochemical along with structural data in order to better understand the function of a previously characterized PPO from
Identifiants
pubmed: 33741634
pii: AEM.00396-21
doi: 10.1128/AEM.00396-21
pmc: PMC8208164
pii:
doi:
Substances chimiques
Fungal Proteins
0
Catechol Oxidase
EC 1.10.3.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2021 American Society for Microbiology.
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