A 2-Tyr-1-carboxylate Mononuclear Iron Center Forms the Active Site of a Paracoccus Dimethylformamidase.


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
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

16961-16966

Subventions

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.

Références

J Biol Chem. 2005 Feb 18;280(7):5820-7
pubmed: 15576371
Appl Microbiol Biotechnol. 2006 Jul;71(3):369-75
pubmed: 16211382
Environ Toxicol Chem. 2012 Mar;31(3):593-604
pubmed: 22169935
Biosci Biotechnol Biochem. 1999 Dec;63(12):2091-6
pubmed: 10664842
J Hazard Mater. 2009 Nov 15;171(1-3):268-72
pubmed: 19592157
Eur J Biochem. 1986 Aug 1;158(3):469-75
pubmed: 3732281
J Mol Biol. 1995 Apr 7;247(4):536-40
pubmed: 7723011
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2256-68
pubmed: 15572779
Toxicol In Vitro. 1994 Jun;8(3):401-6
pubmed: 20692931
Angew Chem Int Ed Engl. 2020 Sep 21;59(39):16961-16966
pubmed: 32452120
Appl Environ Microbiol. 2019 May 30;85(12):
pubmed: 30952664
Toxicol Sci. 2003 Apr;72(2):347-58
pubmed: 12655034
J Biol Chem. 1952 Mar;195(1):141-7
pubmed: 14938362

Auteurs

Chetan Kumar Arya (CK)

Department of Chemistry, Indian Institute of Technology, Kanpur, India.
Institute for Stem Cell Science and Regenerative Medicine, Bangalore, India.

Swati Yadav (S)

National Center for Biological Sciences-TIFR, GKVK Post, Bangalore, India.

Jonathan Fine (J)

Department of Chemistry, Purdue University, West Lafayette, IN, USA.

Ana Casanal (A)

MRC Laboratory of Molecular Biology, Cambridge, UK.

Gaurav Chopra (G)

Department of Chemistry, Purdue University, West Lafayette, IN, USA.

Gurunath Ramanathan (G)

Department of Chemistry, Indian Institute of Technology, Kanpur, India.

Kutti R Vinothkumar (KR)

National Center for Biological Sciences-TIFR, GKVK Post, Bangalore, India.

Ramaswamy Subramanian (R)

Institute for Stem Cell Science and Regenerative Medicine, Bangalore, India.
Department of Biological Sciences and Weldon School of Biomedical Engineering, Purdue University, West Lafayette, IN, USA.

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Classifications MeSH