Maleylpyruvate isomerase

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maleylpyruvate isomerase
Identifiers
EC no. 5.2.1.4
CAS no. 9023-77-2
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MetaCyc metabolic pathway
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In enzymology, a maleylpyruvate isomerase (EC 5.2.1.4) is an enzyme that catalyzes the chemical reaction

3-maleylpyruvate 3-fumarylpyruvate

Hence, this enzyme has one substrate, 3-maleylpyruvate, and one product, 3-fumarylpyruvate.

This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is 3-maleylpyruvate cis-trans-isomerase. This enzyme participates in tyrosine metabolism.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2NSF and 2NSG.

Related Research Articles

In biochemistry, isomerases are a general class of enzymes that convert a molecule from one isomer to another. Isomerases facilitate intramolecular rearrangements in which bonds are broken and formed. The general form of such a reaction is as follows:

<span class="mw-page-title-main">Enoyl CoA isomerase</span> Type of enzyme

Enoyl-CoA-(∆) isomerase (EC 5.3.3.8, also known as dodecenoyl-CoA- isomerase, 3,2-trans-enoyl-CoA isomerase, ∆3 ,∆2 -enoyl-CoA isomerase, or acetylene-allene isomerase, is an enzyme that catalyzes the conversion of cis- or trans-double bonds of coenzyme A bound fatty acids at gamma-carbon to trans double bonds at beta-carbon as below:

<span class="mw-page-title-main">Prolyl isomerase</span> Enzyme

Prolyl isomerase is an enzyme found in both prokaryotes and eukaryotes that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. Proline has an unusually conformationally restrained peptide bond due to its cyclic structure with its side chain bonded to its secondary amine nitrogen. Most amino acids have a strong energetic preference for the trans peptide bond conformation due to steric hindrance, but proline's unusual structure stabilizes the cis form so that both isomers are populated under biologically relevant conditions. Proteins with prolyl isomerase activity include cyclophilin, FKBPs, and parvulin, although larger proteins can also contain prolyl isomerase domains.

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<span class="mw-page-title-main">Maleate isomerase</span>

In enzymology, a maleate isomerase, or maleate cis-tran isomerase, is a member of the Asp/Glu racemase superfamily discovered in bacteria. It is responsible for catalyzing cis-trans isomerization of the C2-C3 double bond in maleate to produce fumarate, which is a critical intermediate in citric acid cycle. The presence of an exogenous mercaptan is required for catalysis to happen.

<span class="mw-page-title-main">Maleylacetoacetate isomerase</span> Class of enzymes

In enzymology, maleylacetoacetate isomerase is an enzyme that catalyzes the chemical reaction

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Prolycopene isomerase is an enzyme with systematic name 7,9,7',9'-tetracis-lycopene cis-trans-isomerase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">3-Maleylpyruvic acid</span> Chemical compound

3-Maleylpyruvic acid, or 3-maleylpyruvate, is a dicarboxylic acid formed by the oxidative ring opening of gentisic acid by gentisate 1,2-dioxygenase during the metabolism of tyrosine. It is converted into 3-fumarylpyruvate by maleylpyruvate isomerase.

<span class="mw-page-title-main">3-Fumarylpyruvic acid</span> Chemical compound

3-Fumarylpyruvic acid, or 3-fumarylpyruvate, is a dicarboxylic acid formed from the isomerisation of 3-maleylpyruvate by maleylpyruvate isomerase. It is converted into fumarate and pyruvate by 3-fumarylpyruvate hydrolase.

References