3-methyl-2-oxobutanoate hydroxymethyltransferase

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3-methyl-2-oxobutanoate hydroxymethyltransferase
Identifiers
EC no. 2.1.2.11
CAS no. 56093-17-5
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BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
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In enzymology, a 3-methyl-2-oxobutanoate hydroxymethyltransferase (EC 2.1.2.11) is an enzyme that catalyzes the chemical reaction

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O tetrahydrofolate + 2-dehydropantoate

The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, 3-methyl-2-oxobutanoate, and H2O, whereas its two products are tetrahydrofolate and 2-dehydropantoate.

This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:3-methyl-2-oxobutanoate hydroxymethyltransferase. Other names in common use include alpha-ketoisovalerate hydroxymethyltransferase, dehydropantoate hydroxymethyltransferase, ketopantoate hydroxymethyltransferase, oxopantoate hydroxymethyltransferase, 5,10-methylene tetrahydrofolate:alpha-ketoisovalerate, and hydroxymethyltransferase. This enzyme participates in pantothenate and coa biosynthesis.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1M3U, 1O66, 1O68, and 1OY0.

Related Research Articles

<span class="mw-page-title-main">Serine hydroxymethyltransferase</span>

Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate (PLP) (Vitamin B6) dependent enzyme (EC 2.1.2.1) which plays an important role in cellular one-carbon pathways by catalyzing the reversible, simultaneous conversions of L-serine to glycine and tetrahydrofolate (THF) to 5,10-Methylenetetrahydrofolate (5,10-CH2-THF). This reaction provides the largest part of the one-carbon units available to the cell.

<span class="mw-page-title-main">5,10-Methylenetetrahydrofolate</span> Chemical compound

5,10-Methylenetetrahydrofolate (N5,N10-Methylenetetrahydrofolate; 5,10-CH2-THF) is cofactor in several biochemical reactions. It exists in nature as the diastereoisomer [6R]-5,10-methylene-THF.

<span class="mw-page-title-main">10-Formyltetrahydrofolate</span> Chemical compound

10-Formyltetrahydrofolate (10-CHO-THF) is a form of tetrahydrofolate that acts as a donor of formyl groups in anabolism. In these reactions 10-CHO-THF is used as a substrate in formyltransferase reactions.

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In enzymology, a ketol-acid reductoisomerase (EC 1.1.1.86) is an enzyme that catalyzes the chemical reaction

In enzymology, a 2-dehydropantoate 2-reductase (EC 1.1.1.169) is an enzyme that catalyzes the chemical reaction

In enzymology, a methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (EC 2.1.1.74) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Thymidylate synthase (FAD)</span>

In enzymology, a thymidylate synthase (FAD) (EC 2.1.1.148) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">3-methyl-2-oxobutanoate dehydrogenase</span> Class of enzymes

In enzymology, a 3-methyl-2-oxobutanoate dehydrogenase (EC 1.2.4.4) is an enzyme that catalyzes the chemical reaction

In enzymology, a (R)-dehydropantoate dehydrogenase (EC 1.2.1.33) is an enzyme that catalyzes the chemical reaction

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In enzymology, a deoxycytidylate 5-hydroxymethyltransferase (EC 2.1.2.8) is an enzyme that catalyzes the chemical reaction

The enzyme 2-dehydropantoate aldolase catalyzes the chemical reaction:

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In enzymology, a 2-isopropylmalate synthase (EC 2.3.3.13) is an enzyme that catalyzes the chemical reaction

In enzymology, a valine-pyruvate transaminase is an enzyme that catalyzes the chemical reaction

In enzymology, a [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Glycine cleavage system</span>

The glycine cleavage system (GCS) is also known as the glycine decarboxylase complex or GDC. The system is a series of enzymes that are triggered in response to high concentrations of the amino acid glycine. The same set of enzymes is sometimes referred to as glycine synthase when it runs in the reverse direction to form glycine. The glycine cleavage system is composed of four proteins: the T-protein, P-protein, L-protein, and H-protein. They do not form a stable complex, so it is more appropriate to call it a "system" instead of a "complex". The H-protein is responsible for interacting with the three other proteins and acts as a shuttle for some of the intermediate products in glycine decarboxylation. In both animals and plants, the glycine cleavage system is loosely attached to the inner membrane of the mitochondria. Mutations in this enzymatic system are linked with glycine encephalopathy.

<span class="mw-page-title-main">Ketopantoic acid</span> Chemical compound

Ketopantoic acid is the organic compound with the formula HOCH2(CH3)2CC(O)CO2H. At physiological conditions, ketopantoic acid exists as its conjugate base, ketopantoate (HOCH2(CH3)2CC(O)CO2).

References