Riboflavin kinase
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In enzymology, a riboflavin kinase () is an
enzyme Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products ...
that catalyzes the
chemical reaction A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the pos ...
:ATP + riboflavin \rightleftharpoons ADP + FMN Thus, the two substrates of this enzyme are ATP and riboflavin, whereas its two
products Product may refer to: Business * Product (business), an item that serves as a solution to a specific consumer problem. * Product (project management), a deliverable or set of deliverables that contribute to a business solution Mathematics * Produ ...
are ADP and FMN. Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase (), which converts it into FMN, and FAD synthetase (), which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme, the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family. The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases. This enzyme belongs to the family of
transferase A transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups (e.g. a methyl or glycosyl group) from one molecule (called the donor) to another (called the acceptor). They are involved in hundreds of ...
s, to be specific, those transferring phosphorus-containing groups ( phosphotransferases) with an alcohol group as acceptor. The
systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivial ...
of this enzyme class is ATP:riboflavin 5'-phosphotransferase. This enzyme is also called flavokinase. This enzyme participates in riboflavin metabolism. However, archaeal riboflavin kinases () in general utilize CTP rather than ATP as the donor nucleotide, catalyzing the reaction :CTP + riboflavin \rightleftharpoons CDP + FMN Riboflavin kinase can also be isolated from other types of bacteria, all with similar function but a different number of amino acids.


Structure

The complete enzyme arrangement can be observed with
X-ray crystallography X-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles ...
and with
NMR Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a strong constant magnetic field are perturbed by a weak oscillating magnetic field (in the near field) and respond by producing an electromagnetic signal with ...
. The riboflavin kinase enzyme isolated from ''
Thermoplasma acidophilum ''Thermoplasma acidophilum'' is an archaeon, the type species of its genus. ''T. acidophilum'' was originally isolated from a self-heating coal refuse pile, at pH 2 and 59 °C. Its genome has been sequenced. It is highly flagellated and gr ...
'' contains 220 amino acids. The structure of this enzyme has been determined
X-ray crystallography X-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles ...
at a resolution of 2.20 Å. Its secondary structure contains 69 residues (30%) in alpha helix form, and 60 residues (26%) a beta sheet conformation. The enzyme contains a
magnesium Magnesium is a chemical element with the symbol Mg and atomic number 12. It is a shiny gray metal having a low density, low melting point and high chemical reactivity. Like the other alkaline earth metals (group 2 of the periodic ta ...
binding site at amino acids 131 and 133, and a
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 we ...
binding site at amino acids 188 and 195. As of late 2007, 14
structures A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or system so organized. Material structures include man-made objects such as buildings and machines and natural objects such as ...
have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , and .


References


Further reading

* * * * * * * {{InterPro content, IPR015865 EC 2.7.1 Enzymes of known structure