Flavin Prenyltransferase (UbiX)
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Flavin Prenyltransferase (UbiX)
UbiX is a flavin prenyltransferase, catalysing the addition of dimethylallyl-monophosphate (DMAP) (or dimethylallyl-pyrophosphate (DMAPP) ) onto the N5 and C6 positions of FMN culminating in the formation of the prenylated FMN ( prFMN) cofactor. The enzyme is involved in the ubiquinone biosynthesis Biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. ... pathway in '' E.coli'' from where it gets its name UbiX is associated with the UbiD enzymes as prFMN is utilised by UbiD enzymes in their function as reversible decarboxylases. Unusually for a prenyltransferase UbiX is not metal dependent. Following the elucidation of prFMN's structure in the active site of Fdc1 from '' aspergillus niger'' (AnFdc1) the prenyltrasferase activity of UbiX was investigated. Incubation of UbiX from '' P. ...
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Dimethylallyl Pyrophosphate
Dimethylallyl pyrophosphate (DMAPP; or alternatively, dimethylallyl diphosphate (DMADP); also isoprenyl pyrophosphate) is an isoprenoid precursor. It is a product of both the mevalonate pathway and the MEP pathway of isoprenoid precursor biosynthesis. It is an isomer of isopentenyl pyrophosphate (IPP) and exists in virtually all life forms. The enzyme isopentenyl pyrophosphate isomerase catalyzes isomerization between DMAPP and IPP. In the mevalonate pathway DMAPP is synthesised from mevalonic acid. In contrast, DMAPP is synthesised from HMBPP in the MEP pathway. At present, it is believed that there is crossover between the two pathways in organisms that use both pathways to create terpenes and terpenoid The terpenoids, also known as isoprenoids, are a class of naturally occurring organic chemicals derived from the 5-carbon compound isoprene and its derivatives called terpenes, diterpenes, etc. While sometimes used interchangeably with "terpenes" ...s, such as in plants, ...
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Flavin Mononucleotide
Flavin mononucleotide (FMN), or riboflavin-5′-phosphate, is a biomolecule produced from riboflavin (vitamin B2) by the enzyme riboflavin kinase and functions as the prosthetic group of various oxidoreductases, including NADH dehydrogenase, as well as cofactor in biological blue-light photo receptors. During the catalytic cycle, a reversible interconversion of the oxidized (FMN), semiquinone (FMNH•), and reduced (FMNH2) forms occurs in the various oxidoreductases. FMN is a stronger oxidizing agent than NAD and is particularly useful because it can take part in both one- and two-electron transfers. In its role as blue-light photo receptor, (oxidized) FMN stands out from the 'conventional' photo receptors as the signaling state and not an E/Z isomerization. It is the principal form in which riboflavin is found in cells and tissues. It requires more energy to produce, but is more soluble than riboflavin. In cells, FMN occurs freely circulating but also in several covalently b ...
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Prenylated Flavin Mononucleotide
Prenylated flavin mononucleotide (prFMN) is a cofactor biosynthesized by the flavin prenyltransferase UbiX and used by UbiD enzymes for reversible decarboxylation reactions. Hence, prFMN is pivotal for catalysis in the ubiquitous microbial UbiD/X system. prFMN is flavin prenylated at the N5 and C6 positions resulting in the formation of a fourth non-aromatic ring. prFMN was discovered in 2015 at the University of Manchester by David Leys' group. : Two studies in 2015 characterized UbiX as a flavin prenyltransferase, supplying prFMN to UbiD/ Fdc1 which utilises the cofactor to catalyse a reversible decarboxylation reaction. Ferulic acid decarboxylase (Fdc1) from ''A. niger'' co-expressed in ''E.coli'' with UbiX from ''E.coli'' (AnFdc1UbiX) once purified had clear spectral differences to singly expressed AnFdc1, and was capable of '' in vitro'' decarboxylation of a range of aromatic carboxylic acids. The atomic resolution of the crystal structure of AnFdc1UbiX, allowed e ...
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Cofactor (biochemistry)
A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction). Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound. Cofactors can be divided into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mostly derived from vitamins and other organic essential nutrients in small amounts. (Note that some scientists limit the use of the term "cofactor" for inorganic substances; both types are included here.) Coenzymes are further divided into two types. The first is called a "prosthetic group", which consists of a coenzyme that is tightly (or even covalently) and permanently bound to a protein. ...
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Ubiquinone
Coenzyme Q, also known as ubiquinone and marketed as CoQ10, is a coenzyme family that is ubiquitous in animals and most bacteria (hence the name ubiquinone). In humans, the most common form is coenzyme Q10 or ubiquinone-10. It is a 1,4-benzoquinone, where Q refers to the quinone chemical group and 10 refers to the number of isoprenyl chemical subunits in its tail. In natural ubiquinones, the number can be anywhere from 6 to 10. This family of fat-soluble substances, which resemble vitamins, is present in all respiring eukaryotic cells, primarily in the mitochondria. It is a component of the electron transport chain and participates in aerobic cellular respiration, which generates energy in the form of ATP. Ninety-five percent of the human body's energy is generated this way. Organs with the highest energy requirements—such as the heart, liver, and kidney—have the highest CoQ10 concentrations. There are three redox states of CoQ: fully oxidized (ubiquinone), semiquinone ...
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Biosynthesis
Biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism. The prerequisite elements for biosynthesis include: precursor compounds, chemical energy (e.g. ATP), and catalytic enzymes which may require coenzymes (e.g.NADH, NADPH). These elements create monomers, the building blocks for macromolecules. Some important biological macromolecules include: proteins, which are composed of amino acid monomers joined via peptide bon ...
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UbiD
uBid.com was an online auction style and fixed-price shopping website offering goods sold directly by the company and items sold by pre-approved third party uBid-certified merchants. The site specialized in excess new, refurbished and overstock consumer electronics such as computers, electronics, home goods, jewelry, watches and cellular phones. History uBid.com was formed and launched in 1997, originally as a subsidiary of PC Mall. In December 1998, during the dot-com bubble, the company became a public company via an initial public offering, and achieved a market capitalization value of over 1.8 billion dollars at one point. After pricing at $15/share, the stock price reached $67 per share on its first day of trading. The company officially spun off from PC Mall with its co-founding management team in 1999. Ownership has changed multiple times over the years. In 2000, CMGI (now Steel Connect) acquired uBid in a stock transaction. In June 2001, the company reached an agreemen ...
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Ferulic Acid Decarboxylase
Ferulic acid decarboxylases (Fdc) are decarboxylase enzymes capable of the reversible decarboxylation of aromatic carboxylic acids such as ferulic acid and cinnamic acid. Fdc's are fungal homologues of the '' E.coli'' UbiD enzyme which is involved in ubiquinone biosynthesis. This places Fdc within the wider UbiD enzyme family, representing a distinct clade within the family Presence of ''fdc1'' and the associated ''pad1'' genes (Pad1 homologous to UbiX in ''E.coli'') were shown to be required for the decarboxylation of phenylacrylic acids in ''Saccharomyces cerevisiae''. In 2015 the cofactor prFMN was discovered in the active site of Fdc1 from '' Aspergillus niger'' (AnFdc) by crystallography, prior to this genetic studies had led to the assumption that both UbiD and UbiX encoded isofunctional decarboxylases. In actuality UbiX/Pad were found to be flavin preyltransferases supplying the prFMN cofactor to UbiD/Fdc where it is utilised for the reversible decarboxylation o ...
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Aspergillus Niger
''Aspergillus niger'' is a mold classified within the ''Nigri'' section of the ''Aspergillus'' genus. The ''Aspergillus'' genus consists of common molds found throughout the environment within soil and water, on vegetation, in fecal matter, on decomposing matter, and suspended in the air. Species within this genus often grow quickly and can sporulate within a few days of germination. A combination of characteristics unique to ''A. niger'' makes the microbe invaluable to the production of many acids, proteins and bioactive compounds. Characteristics including extensive metabolic diversity, high production yield, secretion capability, and the ability to conduct post-translational modifications are responsible for ''A. niger's'' robust production of secondary metabolites. ''A. niger's'' capability to withstand extremely acidic conditions makes it especially important to the industrial production of citric acid. ''A. niger'' causes a disease known as "black mold" on certain fruits an ...
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Sodium Dithionite
Sodium dithionite (also known as sodium hydrosulfite) is a white crystalline powder with a sulfurous odor. Although it is stable in dry air, it decomposes in hot water and in acid solutions. Structure The structure has been examined by Raman spectroscopy and single-crystal X-ray diffraction. The dithionite dianion has C symmetry, with almost eclipsed with a 16° O-S-S-O torsional angle. In the dihydrated form (), the dithionite anion has gauche 56° O-S-S-O torsional angle. A weak S-S bond is indicated by the S-S distance of 239 pm, which is elongated by ca. 30 pm relative to a typical S-S bond. Because this bond is fragile, the dithionite anion dissociates in solution into the O2sup>− radicals, as has been confirmed by EPR spectroscopy. It is also observed that 35S undergoes rapid exchange between S2O42− and SO2 in neutral or acidic solution, consistent with the weak S-S bond in the anion. Preparation Sodium dithionite is produced industrially by reduction of sulfur d ...
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Cellular Respiration
Cellular respiration is the process by which biological fuels are oxidised in the presence of an inorganic electron acceptor such as oxygen to produce large amounts of energy, to drive the bulk production of ATP. Cellular respiration may be described as a set of metabolic reactions and processes that take place in the cells of organisms to convert chemical energy from nutrients into adenosine triphosphate (ATP), and then release waste products. The reactions involved in respiration are catabolic reactions, which break large molecules into smaller ones, releasing energy. Respiration is one of the key ways a cell releases chemical energy to fuel cellular activity. The overall reaction occurs in a series of biochemical steps, some of which are redox reactions. Although cellular respiration is technically a combustion reaction, it is an unusual one because of the slow, controlled release of energy from the series of reactions. Nutrients that are commonly used by animal and plan ...
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Anaerobic Respiration
Anaerobic respiration is respiration using electron acceptors other than molecular oxygen (O2). Although oxygen is not the final electron acceptor, the process still uses a respiratory electron transport chain. In aerobic organisms undergoing respiration, electrons are shuttled to an electron transport chain, and the final electron acceptor is oxygen. Molecular oxygen is an excellent electron acceptor. Anaerobes instead use less-oxidizing substances such as nitrate (), fumarate (), sulfate (), or elemental sulfur (S). These terminal electron acceptors have smaller reduction potentials than O2. Less energy per oxidized molecule is released. Therefore, anaerobic respiration is less efficient than aerobic. As compared with fermentation Anaerobic cellular respiration and fermentation generate ATP in very different ways, and the terms should not be treated as synonyms. Cellular respiration (both aerobic and anaerobic) uses highly reduced chemical compounds such as NADH and FADH2 ( ...
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