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Special Issue "Flavoenzymes"

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (15 November 2017)

Special Issue Editor

Guest Editor
Prof. Dr. Willem van Berkel

Laboratory of Biochemistry, Wageningen University, Stippeneng 4, 6708 WE Wageningen, The Netherlands
Website | E-Mail
Interests: enzyme mechanisms; biocatalysis; redox enzymes; enzyme discovery; enzyme dynamics; protein engineering; protein folding and stability

Special Issue Information

Dear Colleagues,

Flavoenzymes are widespread in nature, constituting about 2% of all enzymes. Using a flavin cofactor, they catalyze a huge variety of redox reactions. Flavoenzymes are attractive biocatalysts because of the selectivity and efficiency of their reactions. Due to their chemical versatility and exquisite regio- and stereoselectivity, flavoenzymes receive much attention in biorganic chemistry, especially for the synthesis of building blocks of chiral and non-chiral drugs and chemicals. Next to that, flavoenzymes are widely used in analytical chemistry, as biosensors, and in food and biorefinery applications. The genomic era has opened up new perspectives on the natural diversity of flavoenzymes and the potential of their unknown characteristics. In addition, ongoing efforts are undertaken to advance structure-function relationships of flavoenzymes. The present Special Issue is aimed at the description of new flavoenzymes and their cofactors, the engineering and evolution of flavoenzymes, as well as their novel applications.

Prof. Dr. Willem van Berkel
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • flavin
  • flavoenzyme
  • discovery
  • mechanism
  • biocatalysis
  • engineering

Published Papers (1 paper)

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Research

Open AccessArticle Characterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesis
Molecules 2017, 22(10), 1652; doi:10.3390/molecules22101652
Received: 7 September 2017 / Revised: 27 September 2017 / Accepted: 28 September 2017 / Published: 1 October 2017
PDF Full-text (1739 KB) | HTML Full-text | XML Full-text
Abstract
N-Hydroxylating monooxygenases (NMOs) are involved in siderophore biosynthesis. Siderophores are high affinity iron chelators composed of catechol and hydroxamate functional groups that are synthesized and secreted by microorganisms and plants. Recently, a new siderophore named albachelin was isolated from a culture of
[...] Read more.
N-Hydroxylating monooxygenases (NMOs) are involved in siderophore biosynthesis. Siderophores are high affinity iron chelators composed of catechol and hydroxamate functional groups that are synthesized and secreted by microorganisms and plants. Recently, a new siderophore named albachelin was isolated from a culture of Amycolatopsis alba growing under iron-limiting conditions. This work focuses on the expression, purification, and characterization of the NMO, abachelin monooxygenase (AMO) from A. alba. This enzyme was purified and characterized in its holo (FAD-bound) and apo (FAD-free) forms. The apo-AMO could be reconstituted by addition of free FAD. The two forms of AMO hydroxylate ornithine, while lysine increases oxidase activity but is not hydroxylated and display low affinity for NADPH. Full article
(This article belongs to the Special Issue Flavoenzymes)
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