ArticleActa crystallographica. Section D, Biological crystallography2015
The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer-Villiger monooxygenase.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- The Role of Dioxygen in Microbial Bio-Oxygenation: Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme.Microorganisms · 2024Review
- Structure and Function of the α-Hydroxylation Bimodule of the Mupirocin Polyketide Synthase.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- Structure and Function of the α-Hydroxylation Bimodule of the Mupirocin Polyketide Synthase.Angewandte Chemie (International ed. in English) · 2023Article
- Formicamycin biosynthesis involves a unique reductive ring contraction.Chemical science · 2020Article
- Conferring the Metabolic Self-Sufficiency of the CAM Plasmid ofMicroorganisms · 2019Article
- Characterised Flavin-Dependent Two-Component Monooxygenases from the CAM Plasmid ofMicroorganisms · 2018Review
- Reconstructing the evolutionary history of FScientific reports · 2018Article
- Reply to the Comment by Littlechild and Isupov.Microorganisms · 2017Article
- Comments to Article by Willetts A. et al., Microorganisms 2016, 4, 38.Microorganisms · 2017Article
- Article
- Flavin-Dependent Redox Transfers by the Two-Component Diketocamphane Monooxygenases of Camphor-Grown Pseudomonas putida NCIMB 10007.Microorganisms · 2016Article
Corrections and comments
- Erratum issued
Authors and funding
18 authors at 5 institutions in 4 countries.
Funding
Abstract
The three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer-Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 Å resolution. The structure of this dimeric FMN-dependent enzyme, which is encoded on the large CAM plasmid of Pseudomonas putida, has been solved by a combination of multiple anomalous dispersion from a bromine crystal soak and molecular replacement using a bacterial luciferase model. The orientation of the isoalloxazine ring of the FMN cofactor in the active site of this TIM-barrel fold enzyme differs significantly from that previously observed in enzymes of the bacterial luciferase-like superfamily. The Ala77 residue is in a cis conformation and forms a β-bulge at the C-terminus of β-strand 3, which is a feature observed in many proteins of this superfamily.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.