Trapping conformational states of a flavin-dependent

Aspergillus fumigatus / enzymology Catalytic Domain Crystallography, X-Ray Flavin-Adenine Dinucleotide / chemistry Fungal Proteins / chemistry Mixed Function Oxygenases / chemistry NADP / chemistry Ornithine / chemistry
X-ray crystallography enzyme kinetics enzyme structure flavin-dependent monooxygenases flavoprotein ornithine hydroxylase siderophore site-directed mutagenesis

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
18 09 2020
Historique:
received: 23 06 2020
revised: 21 07 2020
pubmed: 30 7 2020
medline: 27 1 2021
entrez: 30 7 2020
Statut: ppublish

Résumé

The siderophore biosynthetic enzyme A (SidA) ornithine hydroxylase from

Identifiants

DOI: 10.1074/jbc.RA120.014750 PMID: 32723870 PMC: PMC7504930
pubmed: 32723870
pii: S0021-9258(17)50040-X
doi: 10.1074/jbc.RA120.014750
pmc: PMC7504930
pii:
doi:

Substances chimiques

Fungal Proteins 0
Flavin-Adenine Dinucleotide 146-14-5
NADP 53-59-8
Ornithine E524N2IXA3
Mixed Function Oxygenases EC 1.-

Banques de données

PDB
['4B69', '4TM3', '4TLZ', '4TLX', '6X0I', '6X0H', '4B63']

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

Pagination

13239-13249

Subventions

Organisme : NIGMS NIH HHS
ID : P30 GM124165
Pays : United States
Organisme : NIGMS NIH HHS
ID : P30 GM124169
Pays : United States
Organisme : NIH HHS
ID : S10 OD021527
Pays : United States
Organisme : NCRR NIH HHS
ID : S10 RR029205
Pays : United States

Informations de copyright

© 2020 Campbell et al.

Déclaration de conflit d'intérêts

Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.

Références

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Auteurs

Ashley C Campbell (AC)

Department of Biochemistry, University of Missouri, Columbia, Missouri, USA.

Kyle M Stiers (KM)

Department of Biochemistry, University of Missouri, Columbia, Missouri, USA.

Julia S Martin Del Campo (JS)

Department of Biochemistry, Virginia Tech, Blacksburg, Virginia, USA.

Ritcha Mehra-Chaudhary (R)

Department of Biochemistry, University of Missouri, Columbia, Missouri, USA.

Pablo Sobrado (P)

Department of Biochemistry, Virginia Tech, Blacksburg, Virginia, USA. Electronic address: psobrado@vt.edu.

John J Tanner (JJ)

Department of Biochemistry, University of Missouri, Columbia, Missouri, USA; Department of Chemistry, University of Missouri, Columbia, Missouri, USA. Electronic address: tannerjj@missouri.edu.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Champignons › Deuteromycota › Aspergillus › Aspergillus fumigatus › Trapping conformational states of a flavin-dependent
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Éléments structuraux des protéines › Domaine catalytique › Trapping conformational states of a flavin-dependent
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Cristallographie aux rayons X › Trapping conformational states of a flavin-dependent
questionsmedicales.fr › Facteurs biologiques › Pigments biologiques › Flavines › Riboflavine › Flavine adénine dinucléotide › Trapping conformational states of a flavin-dependent
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines fongiques › Trapping conformational states of a flavin-dependent
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Oxidoreductases › Oxygénases › Mixed function oxygenases › Trapping conformational states of a flavin-dependent
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Nucléotides › Ribonucléotides › Nucléotides adényliques › NADP › Trapping conformational states of a flavin-dependent
questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Acides aminés diaminés › Ornithine › Trapping conformational states of a flavin-dependent