Methylenetetrahydromethanopterin dehydrogenase
Encyclopedia
In enzymology, a methylenetetrahydromethanopterin dehydrogenase is an enzyme
that catalyzes
the chemical reaction
Thus, the two substrates
of this enzyme are 5,10-methylenetetrahydromethanopterin and coenzyme F420
, whereas its two products
are 5,10-methenyltetrahydromethanopterin and reduced coenzyme F420.
This enzyme belongs to the family of oxidoreductase
s, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is 5,10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase. Other names in common use include N5,N10-methylenetetrahydromethanopterin dehydrogenase, and 5,10-methylenetetrahydromethanopterin dehydrogenase. This enzyme participates in folate biosynthesis.
have been solved for this class of enzymes, with PDB
accession codes , , , and .
Enzyme
Enzymes are proteins that catalyze chemical reactions. In enzymatic reactions, the molecules at the beginning of the process, called substrates, are converted into different molecules, called products. Almost all chemical reactions in a biological cell need enzymes in order to occur at rates...
that catalyzes
Catalysis
Catalysis is the change in rate of a chemical reaction due to the participation of a substance called a catalyst. Unlike other reagents that participate in the chemical reaction, a catalyst is not consumed by the reaction itself. A catalyst may participate in multiple chemical transformations....
the chemical reaction
Chemical reaction
A chemical reaction is a process that leads to the transformation of one set of chemical substances to another. Chemical reactions can be either spontaneous, requiring no input of energy, or non-spontaneous, typically following the input of some type of energy, such as heat, light or electricity...
- 5,10-methylenetetrahydromethanopterin + coenzyme F420
5,10-methenyltetrahydromethanopterin + reduced coenzyme F420
Thus, the two substrates
Substrate (biochemistry)
In biochemistry, a substrate is a molecule upon which an enzyme acts. Enzymes catalyze chemical reactions involving the substrate. In the case of a single substrate, the substrate binds with the enzyme active site, and an enzyme-substrate complex is formed. The substrate is transformed into one or...
of this enzyme are 5,10-methylenetetrahydromethanopterin and coenzyme F420
Coenzyme F420
Coenzyme F420 or 8-hydroxy-5-deazaflavin is a coenzyme involved in redox reactions in methanogens , in many Actinobacteria, and sporadically in other bacterial lineages. It is a flavin derivative...
, whereas its two products
Product (chemistry)
Product are formed during chemical reactions as reagents are consumed. Products have lower energy than the reagents and are produced during the reaction according to the second law of thermodynamics. The released energy comes from changes in chemical bonds between atoms in reagent molecules and...
are 5,10-methenyltetrahydromethanopterin and reduced coenzyme F420.
This enzyme belongs to the family of oxidoreductase
Oxidoreductase
In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule to another...
s, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is 5,10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase. Other names in common use include N5,N10-methylenetetrahydromethanopterin dehydrogenase, and 5,10-methylenetetrahydromethanopterin dehydrogenase. This enzyme participates in folate biosynthesis.
Structural studies
As of late 2007, 4 structuresTertiary structure
In biochemistry and molecular biology, the tertiary structure of a protein or any other macromolecule is its three-dimensional structure, as defined by the atomic coordinates.-Relationship to primary structure:...
have been solved for this class of enzymes, with PDB
Protein Data Bank
The Protein Data Bank is a repository for the 3-D structural data of large biological molecules, such as proteins and nucleic acids....
accession codes , , , and .