Marco Wilhelmus Fraaije (born 7 December 1968) is a Dutch scientist whose research concerns enzymology of redox enzymes, enzyme discovery & engineering and biocatalysis at the Groningen Biomolecular Sciences and Biotechnology Institute (GBB) at the University of Groningen. [1] [2] [3] [4]
Marco Fraaije graduated in 1993 with a Master of Science degree in Molecular Sciences at Wageningen University. [5] Subsequently, he became a doctoral student at Wageningen University under supervision of Willem van Berkel focusing on the mechanism and structure of flavoenzymes and was awarded his PhD in biochemistry in 1998. [6] Following his PhD, he worked as a postdoctoral researcher as EMBO fellow in the protein crystallography research group at the University of Pavia. In 1999, he was made assistant professor at GBB at the University of Groningen, and in 2007 he was appointed as associate professor. In 2012, he was made full professor in molecular enzymology. [5]
Fraaije is active in the fields of enzyme engineering and biocatalysis. [1] His research mainly deals with discovery, engineering and exploration of novel oxidative enzymes, with special emphasis on flavin-containing enzymes. [7] Besides exploring the biocatalytic potential of these biocatalysts, he also aims at elucidating the molecular functioning of oxidative flavoenzymes. [2] He also has interest in evolutionary aspects of enzymology and in line with this he is board member of the geological museum Oertijdmuseum in Boxtel. [8]
Marco Fraaije has a significant number of publications and four patents. [1] [9] He has coordinated EU-funded projects including OXYGREEN (2008-2013), [10] ROBOX (2015-2019), [11] and OXYTRAIN (2017-2020). [12]
In 2018, Fraaije received the BIOCAT science award from the Biocat Society at the International Congress on Biocatalysis for his scientific achievement in the field of biocatalysis. [13] Other research prizes include the Unilever research prize, 1993; EMBO long-term fellowship, 1998; and the VICI-NWO research grant, 2016. [5]
In 2005, he became a member of the Biomolecular Chemistry division of the Netherlands Organization for Scientific Research and currently chairs the Applied Biocatalysis division of the Dutch Biotechnology Society. [14]
A dehydrogenase is an enzyme belonging to the group of oxidoreductases that oxidizes a substrate by reducing an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN. Like all catalysts, they catalyze reverse as well as forward reactions, and in some cases this has physiological significance: for example, alcohol dehydrogenase catalyzes the oxidation of ethanol to acetaldehyde in animals, but in yeast it catalyzes the production of ethanol from acetaldehyde.
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN). Many flavoproteins are known: components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase complex.
Methylotrophs are a diverse group of microorganisms that can use reduced one-carbon compounds, such as methanol or methane, as the carbon source for their growth; and multi-carbon compounds that contain no carbon-carbon bonds, such as dimethyl ether and dimethylamine. This group of microorganisms also includes those capable of assimilating reduced one-carbon compounds by way of carbon dioxide using the ribulose bisphosphate pathway. These organisms should not be confused with methanogens which on the contrary produce methane as a by-product from various one-carbon compounds such as carbon dioxide. Some methylotrophs can degrade the greenhouse gas methane, and in this case they are called methanotrophs. The abundance, purity, and low price of methanol compared to commonly used sugars make methylotrophs competent organisms for production of amino acids, vitamins, recombinant proteins, single-cell proteins, co-enzymes and cytochromes.
The Baeyer–Villiger oxidation is an organic reaction that forms an ester from a ketone or a lactone from a cyclic ketone, using peroxyacids or peroxides as the oxidant. The reaction is named after Adolf von Baeyer and Victor Villiger who first reported the reaction in 1899.
Biocatalysis refers to the use of living (biological) systems or their parts to speed up (catalyze) chemical reactions. In biocatalytic processes, natural catalysts, such as enzymes, perform chemical transformations on organic compounds. Both enzymes that have been more or less isolated and enzymes still residing inside living cells are employed for this task. Modern biotechnology, specifically directed evolution, has made the production of modified or non-natural enzymes possible. This has enabled the development of enzymes that can catalyze novel small molecule transformations that may be difficult or impossible using classical synthetic organic chemistry. Utilizing natural or modified enzymes to perform organic synthesis is termed chemoenzymatic synthesis; the reactions performed by the enzyme are classified as chemoenzymatic reactions.
Oxidative deamination is a form of deamination that generates α-keto acids and other oxidized products from amine-containing compounds, and occurs primarily in the liver. Oxidative deamination is stereospecific, meaning it contains different stereoisomers as reactants and products; this process is either catalyzed by L or D- amino acid oxidase and L-amino acid oxidase is present only in the liver and kidney. Oxidative deamination is an important step in the catabolism of amino acids, generating a more metabolizable form of the amino acid, and also generating ammonia as a toxic byproduct. The ammonia generated in this process can then be neutralized into urea via the urea cycle.
D-amino-acid dehydrogenase is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors. The enzyme has a very broad specificity and can act on most D-amino acids.
In enzymology, a 4-hydroxyacetophenone monooxygenase (EC 1.14.13.84) is an enzyme that catalyzes the chemical reaction:
In enzymology, a phenylacetone monooxygenase (EC 1.14.13.92) is an enzyme that catalyzes the chemical reaction
In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction
Long-chain alcohol oxidase is one of two enzyme classes that oxidize long-chain or fatty alcohols to aldehydes. It has been found in certain Candida yeast, where it participates in omega oxidation of fatty acids to produce acyl-CoA for energy or industrial use, as well as in other fungi, plants, and bacteria.
A polyamine oxidase (PAO) is an enzymatic flavoprotein that oxidizes a carbon-nitrogen bond in a secondary amino group of a polyamine donor, using molecular oxygen as an acceptor. The generalized PAO reaction converts three substrates into three products. Different PAOs with varying substrate specificities exist in different organisms. Phylogenetic analyses suggest that PAOs likely evolved once in eukaryotes and diversified by divergent evolution and gene duplication events, though some prokaryotes have acquired PAOs through horizontal gene transfer.
In molecular biology, the FAD dependent oxidoreductase family of proteins is a family of FAD dependent oxidoreductases. Members of this family include Glycerol-3-phosphate dehydrogenase EC 1.1.99.5, Sarcosine oxidase beta subunit EC 1.5.3.1, D-amino-acid dehydrogenase EC 1.4.99.1, D-aspartate oxidase EC 1.4.3.1.
In molecular biology FAD-oxidases are a family of FAD-dependent oxidoreductases. They are flavoproteins that contain a covalently bound FAD group which is attached to a histidine via an 8-alpha-(N3-histidyl)-riboflavin linkage. The region around the histidine that binds the FAD group is conserved in these enzymes.
A styrene monooxygenase (SMO; EC 1.14.14.11) is an enzyme that catalyzes the chemical reaction
The flavin-containing monooxygenase (FMO) protein family specializes in the oxidation of xeno-substrates in order to facilitate the excretion of these compounds from living organisms. These enzymes can oxidize a wide array of heteroatoms, particularly soft nucleophiles, such as amines, sulfides, and phosphites. This reaction requires an oxygen, an NADPH cofactor, and an FAD prosthetic group. FMOs share several structural features, such as a NADPH binding domain, FAD binding domain, and a conserved arginine residue present in the active site. Recently, FMO enzymes have received a great deal of attention from the pharmaceutical industry both as a drug target for various diseases and as a means to metabolize pro-drug compounds into active pharmaceuticals. These monooxygenases are often misclassified because they share activity profiles similar to those of cytochrome P450 (CYP450), which is the major contributor to oxidative xenobiotic metabolism. However, a key difference between the two enzymes lies in how they proceed to oxidize their respective substrates; CYP enzymes make use of an oxygenated heme prosthetic group, while the FMO family utilizes FAD to oxidize its substrates.
A smart cosubstrate is a type of cosubstrate used for cofactor regeneration to yield greater productivity and lower environmental impact (E-factor). A good example of a smart cosubstrate is a lactonizable diol.
Berberine bridge enzyme-like form a subgroup of the superfamily of FAD-linked oxidases, structurally characterized by a typical fold observed initially for vanillyl-alcohol oxidase (VAO). This proteins are part of a multigene family (PF08031) that can be found in plants, fungi and bacteria.
Nicholas John Turner, is a British chemist and a Professor in the Department of Chemistry at The University of Manchester. His research in general is based on biochemistry and organic chemistry, specifically on biotechnology, cell biology, biocatalysis and organic synthesis.
Selin Kara is a Turkish-born chemist and biotechnologist. She is currently a full professor and head of Industrial Biotechnology section at Aarhus University. She studies biocatalysis and has been recognized for her work about deep eutectic solvents and her research regarding cofactor regeneration in biotransformations.
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