The Mechanism of Enzymatic Action

A special issue of Biology (ISSN 2079-7737).

Deadline for manuscript submissions: closed (30 December 2017) | Viewed by 13671

Special Issue Editor


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Guest Editor
Istituto di Chimica Biomolecolare, Consiglio Nazionale delle Ricerche, Comprensorio Olivetti, Edificio 70, Via Campi Flegrei 34, I-80078 Pozzuoli, Napoli, Italy
Interests: biocatalysis; marine enzymes; marine glycosidases; marine biotechnology; oligosaccharides
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Special Issue Information

Dear Colleagues,

The molecular aspects of enzymatic actions are of fundamental scientific interest; they are simply related to protein chemistry and to substrate/product molecules, including, also, all aspects of the chemistry of the reaction, such as solvents, temperature, etc. It could seem an evergreen topic since beginning of disciplines such as biochemistry, organic chemistry, etc. of the last century, and as such a special issue dedicated to it could be considered no more than remembrance of good old times.

However, recent discovery of new environments, inhabited by unknown micro- and macroorganisms, has provided new scientific subjects in terms of fundamental and applied science, in the marine and extreme domains of remote regions of the globe, as the most promising pillars.

Therefore, reviewing and focusing on the mechanisms of enzymatic action seems again appropriate, providing a broadened significance of the terms. In terms of fundamental science, bioprocesses of new enzymes from unknown habitats are characterized by unique aspects based on (i) habitat-related properties (salt tolerance, hyperthermostability, barophilicity, cold adaptivity, etc.) and on (ii) molecular aspects, such as new stereochemistry. In terms of applied science, the title of this Special Issue should be considered under the (bio)technological aspects of enzymatic catalysis, acquiring the widest significance in such a way that chemists, biologists, etc., could contribute to the molecularity of catalysis on the one hand, and engineers and biotechnologists, for product quality and technological aspects of bioprocesses, on the other hand.

In this Special Issue articles or reviews concerning molecular and technological aspects of enzymatic action are expected in order to discuss more recent discoveries in new biocatalysts.

As the Guest Editor, I invite researchers from industry and academia, working with enzymes, to describe recent advances in the field.

Dr. Antonio Trincone
Guest Editor

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Keywords

  • Biocatalysts
  • Enzymes
  • Bioprocesses
  • Applied biology
  • Biomolecular and metabolic engineering

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Published Papers (1 paper)

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Review

35 pages, 5657 KiB  
Review
Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities
by Thomas Heine, Willem J. H. Van Berkel, George Gassner, Karl-Heinz Van Pée and Dirk Tischler
Biology 2018, 7(3), 42; https://doi.org/10.3390/biology7030042 - 2 Aug 2018
Cited by 79 | Viewed by 11665
Abstract
Flavoprotein monooxygenases create valuable compounds that are of high interest for the chemical, pharmaceutical, and agrochemical industries, among others. Monooxygenases that use flavin as cofactor are either single- or two-component systems. Here we summarize the current knowledge about two-component flavin adenine dinucleotide (FAD)-dependent [...] Read more.
Flavoprotein monooxygenases create valuable compounds that are of high interest for the chemical, pharmaceutical, and agrochemical industries, among others. Monooxygenases that use flavin as cofactor are either single- or two-component systems. Here we summarize the current knowledge about two-component flavin adenine dinucleotide (FAD)-dependent monooxygenases and describe their biotechnological relevance. Two-component FAD-dependent monooxygenases catalyze hydroxylation, epoxidation, and halogenation reactions and are physiologically involved in amino acid metabolism, mineralization of aromatic compounds, and biosynthesis of secondary metabolites. The monooxygenase component of these enzymes is strictly dependent on reduced FAD, which is supplied by the reductase component. More and more representatives of two-component FAD-dependent monooxygenases have been discovered and characterized in recent years, which has resulted in the identification of novel physiological roles, functional properties, and a variety of biocatalytic opportunities. Full article
(This article belongs to the Special Issue The Mechanism of Enzymatic Action)
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