A shared mechanistic pathway for pyridoxal phosphate-dependent arginine oxidases.
X-ray crystallography
molecular dynamics
oxidase
pyridoxal phosphate
water
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
05 10 2021
05 10 2021
Historique:
accepted:
21
07
2021
entrez:
28
9
2021
pubmed:
29
9
2021
medline:
15
12
2021
Statut:
ppublish
Résumé
The mechanism by which molecular oxygen is activated by the organic cofactor pyridoxal phosphate (PLP) for oxidation reactions remains poorly understood. Recent work has identified arginine oxidases that catalyze desaturation or hydroxylation reactions. Here, we investigate a desaturase from the
Identifiants
pubmed: 34580201
pii: 2012591118
doi: 10.1073/pnas.2012591118
pmc: PMC8501904
pii:
doi:
Substances chimiques
Pyridoxal Phosphate
5V5IOJ8338
Mixed Function Oxygenases
EC 1.-
Amino Acid Oxidoreductases
EC 1.4.-
arginine oxidase
EC 1.4.3.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM124480
Pays : United States
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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