A 2-Tyr-1-carboxylate Mononuclear Iron Center Forms the Active Site of a Paracoccus Dimethylformamidase.
amide bond hydrolysis
bioremediation
dimethylforamamidase
metalloenzymes
protein structure
Journal
Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543
Informations de publication
Date de publication:
21 09 2020
21 09 2020
Historique:
received:
12
04
2020
revised:
04
05
2020
pubmed:
27
5
2020
medline:
19
3
2021
entrez:
27
5
2020
Statut:
ppublish
Résumé
N,N-dimethyl formamide (DMF) is an extensively used organic solvent but is also a potent pollutant. Certain bacterial species from genera such as Paracoccus, Pseudomonas, and Alcaligenes have evolved to use DMF as a sole carbon and nitrogen source for growth via degradation by a dimethylformamidase (DMFase). We show that DMFase from Paracoccus sp. strain DMF is a halophilic and thermostable enzyme comprising a multimeric complex of the α
Identifiants
pubmed: 32452120
doi: 10.1002/anie.202005332
pmc: PMC7686228
mid: NIHMS1624783
doi:
Substances chimiques
Tyrosine
42HK56048U
Dimethylformamide
8696NH0Y2X
Amidohydrolases
EC 3.5.-
N,N-dimethylformamidase
EC 3.5.1.-
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
Pagination
16961-16966Subventions
Organisme : Medical Research Council
ID : MC_U105192715
Pays : United Kingdom
Organisme : NCI NIH HHS
ID : P30 CA023168
Pays : United States
Organisme : NCATS NIH HHS
ID : UL1 TR002529
Pays : United States
Informations de copyright
© 2020 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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