Threonine synthase

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threonine synthase
2c2g.jpg
threonine synthase dimer, Arabidopsis thaliana
Identifiers
EC number 4.2.3.1
CAS number 9023-97-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, a threonine synthase (EC 4.2.3.1) is an enzyme that catalyzes the chemical reaction

The Enzyme Commission number is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.

Catalysis chemical process

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which is not consumed in the catalyzed reaction and can continue to act repeatedly. Because of this, only very small amounts of catalyst are required to alter the reaction rate in principle.

Chemical reaction Process that results in the interconversion of chemical species

A chemical reaction is a process that leads to the chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the positions of electrons in the forming and breaking of chemical bonds between atoms, with no change to the nuclei, and can often be described by a chemical equation. Nuclear chemistry is a sub-discipline of chemistry that involves the chemical reactions of unstable and radioactive elements where both electronic and nuclear changes can occur.

O-phospho-L-homoserine + H2O L-threonine + phosphate

Thus, the two substrates of this enzyme are O-phospho-L-homoserine and H2O, whereas its two products are L-threonine and phosphate.

Water Chemical compound with formula H2O

Water is a transparent, tasteless, odorless, and nearly colorless chemical substance, which is the main constituent of Earth's streams, lakes, and oceans, and the fluids of most living organisms. It is vital for all known forms of life, even though it provides no calories or organic nutrients. Its chemical formula is H2O, meaning that each of its molecules contains one oxygen and two hydrogen atoms, connected by covalent bonds. Water is the name of the liquid state of H2O at standard ambient temperature and pressure. It forms precipitation in the form of rain and aerosols in the form of fog. Clouds are formed from suspended droplets of water and ice, its solid state. When finely divided, crystalline ice may precipitate in the form of snow. The gaseous state of water is steam or water vapor. Water moves continually through the water cycle of evaporation, transpiration (evapotranspiration), condensation, precipitation, and runoff, usually reaching the sea.

Products are the species formed from chemical reactions. During a chemical reaction reactants are transformed into products after passing through a high energy transition state. This process results in the consumption of the reactants. It can be a spontaneous reaction or mediated by catalysts which lower the energy of the transition state, and by solvents which provide the chemical environment necessary for the reaction to take place. When represented in chemical equations products are by convention drawn on the right-hand side, even in the case of reversible reactions. The properties of products such as their energies help determine several characteristics of a chemical reaction such as whether the reaction is exergonic or endergonic. Additionally the properties of a product can make it easier to extract and purify following a chemical reaction, especially if the product has a different state of matter than the reactants. Reactants are molecular materials used to create chemical reactions. The atoms aren't created or destroyed. The materials are reactive and reactants are rearranging during a chemical reaction. Here is an example of reactants: CH4 + O2. A non-example is CO2 + H2O or "energy".

Phosphate salt or ester of phosphoric acid

A Phosphate is a chemical derivative of phosphoric acid. The phosphate ion (PO
4
)3−
is an inorganic chemical, the conjugate base that can form many different salts. In organic chemistry, a phosphate, or organophosphate, is an ester of phosphoric acid. Of the various phosphoric acids and phosphates, organic phosphates are important in biochemistry and biogeochemistry, and inorganic phosphates are mined to obtain phosphorus for use in agriculture and industry. At elevated temperatures in the solid state, phosphates can condense to form pyrophosphates.

This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is O-phospho-L-homoserine phosphate-lyase (adding water L-threonine-forming). Other names in common use include threonine synthetase, and O-phospho-L-homoserine phospho-lyase (adding water). This enzyme participates in glycine, serine and threonine metabolism and vitamin B6 metabolism. It employs one cofactor, pyridoxal phosphate.

In biochemistry, a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible. For example, an enzyme that catalyzed this reaction would be a lyase:

Vitamin B<sub>6</sub> class of chemically related vitamins

Vitamin B6 refers to a group of chemically similar compounds which can be interconverted in biological systems. Vitamin B6 is part of the vitamin B group of essential nutrients. Its active form, pyridoxal 5′-phosphate, serves as a coenzyme in some 100 enzyme reactions in amino acid, glucose, and lipid metabolism.

Cofactor (biochemistry) a non-protein chemical compound or metallic ion that is required for a proteins biological activity to happen

A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's activity as a catalyst, 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 by in an area of study called enzyme kinetics.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1UIM, 1UIN, 1V7C, 1VB3, 2C2B, 2C2G, and 2D1F.

The Protein Data Bank (PDB) is a database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids. The data, typically obtained by X-ray crystallography, NMR spectroscopy, or, increasingly, cryo-electron microscopy, and submitted by biologists and biochemists from around the world, are freely accessible on the Internet via the websites of its member organisations. The PDB is overseen by an organization called the Worldwide Protein Data Bank, wwPDB.

Related Research Articles

Amino acid synthesis complementary food consist of

Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can only synthesize 11 of the 20 standard amino acids, and in time of accelerated growth, histidine, can be considered an essential amino acid.

AIR synthetase is the fifth enzyme in the de novo synthesis of purine nucleotides. It catalyzes the reaction to form 5-aminoimidazole ribotide (AIR) from formylglycinamidine-ribonucleotide FGAM. This reaction closes the ring and produces a 5-membered imidazole ring of the purine nucleus (AIR):

Purine metabolism refers to the metabolic pathways to synthesize and break down purines that are present in many organisms.

Transsulfuration pathway

The transsulfuration pathway is a metabolic pathway involving the interconversion of cysteine and homocysteine through the intermediate cystathionine. This is in contrast to the direct sulfurylation pathways for the synthesis of cysteine or homocysteine via the replacement of the acetyl/succinyl group with free sulfide. Two transsulfurylation pathways are known: the forward and the reverse.

L-serine ammonia-lyase class of enzymes

In enzymology, a L-serine ammonia-lyase (EC 4.3.1.17) is an enzyme that catalyzes the chemical reaction

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Phosphoribosylaminoimidazolesuccinocarboxamide synthase class of enzymes

In molecular biology, the protein domain SAICAR synthase is an enzyme which catalyses a reaction to create SAICAR. In enzymology, this enzyme is also known as phosphoribosylaminoimidazolesuccinocarboxamide synthase. It is an enzyme that catalyzes the chemical reaction

Phosphoribosylformylglycinamidine synthase enzyme

In enzymology, a phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) is an enzyme that catalyzes the chemical reaction

In enzymology, an ethanolamine-phosphate phospho-lyase (EC 4.2.3.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a pseudouridylate synthase (EC 4.2.1.70) is an enzyme that catalyzes the chemical reaction

In enzymology, a phosphoserine phosphatase (EC 3.1.3.3) is an enzyme that catalyzes the following chemical reaction:

In enzymology, a 3-deoxy-8-phosphooctulonate synthase (EC 2.5.1.55) is an enzyme that catalyzes the chemical reaction

In enzymology, a cystathionine gamma-synthase (EC 2.5.1.48) is an enzyme that catalyzes the formation of cystathionine from cysteine and an activated derivative of homoserine, e.g.:

In enzymology, a cysteine synthase (EC 2.5.1.47) is an enzyme that catalyzes the chemical reaction

In enzymology, a N-acylneuraminate-9-phosphate synthase (EC 2.5.1.57) is an enzyme that catalyzes the chemical reaction

In enzymology, an O-phosphoserine sulfhydrylase is an enzyme that catalyzes the chemical reaction

In enzymology, a CDP-diacylglycerol—serine O-phosphatidyltransferase is an enzyme that catalyzes the chemical reaction

Homoserine kinase class of enzymes

In enzymology, a homoserine kinase is an enzyme that catalyzes the chemical reaction

DAHP synthase class of enzymes

3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. Since it is the first enzyme in the shikimate pathway, it controls the amount of carbon entering the pathway. Enzyme inhibition is the primary method of regulating the amount of carbon entering the pathway. Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme.

References