Insight into multicopper oxidase laccase from
Amino Acid Sequence
Ampyrone
/ metabolism
Benzothiazoles
/ metabolism
Bilirubin
/ metabolism
Computer Simulation
Fungal Proteins
/ chemistry
Guaiacol
/ metabolism
Hydrazones
/ metabolism
Hydrogen-Ion Concentration
Hypocreales
/ enzymology
Laccase
/ chemistry
Molecular Docking Simulation
Oxidoreductases
/ chemistry
Oxidoreductases Acting on CH-CH Group Donors
/ chemistry
Phenol
/ metabolism
Protein Conformation
Pyrogallol
/ analogs & derivatives
Substrate Specificity
Sulfonic Acids
/ metabolism
Bilirubin oxidase
docking
laccase
phenol
resorcinol
Journal
Journal of environmental science and health. Part. B, Pesticides, food contaminants, and agricultural wastes
ISSN: 1532-4109
Titre abrégé: J Environ Sci Health B
Pays: England
ID NLM: 7607167
Informations de publication
Date de publication:
2020
2020
Historique:
pubmed:
3
9
2020
medline:
17
2
2021
entrez:
3
9
2020
Statut:
ppublish
Résumé
The oxidation activity of multicopper-oxidases overlaps with different substrates of laccases and bilirubin oxidases, thus in the present study an integrated approach of bioinformatics using homology modeling, docking, and experimental validation was used to confirm the type of multicopper-oxidase in
Identifiants
pubmed: 32877269
doi: 10.1080/03601234.2020.1812334
doi:
Substances chimiques
Benzothiazoles
0
Fungal Proteins
0
Hydrazones
0
Sulfonic Acids
0
Pyrogallol
01Y4A2QXY0
Ampyrone
0M0B7474RA
syringaldazine
14414-32-5
2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid
28752-68-3
Phenol
339NCG44TV
pyrogallol 1,3-dimethyl ether
4UQT464H8K
Guaiacol
6JKA7MAH9C
Oxidoreductases
EC 1.-
Laccase
EC 1.10.3.2
copper oxidase
EC 1.16.-
Oxidoreductases Acting on CH-CH Group Donors
EC 1.3.-
bilirubin oxidase
EC 1.3.3.5
Bilirubin
RFM9X3LJ49
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM