Chloromuconate cycloisomerase

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chloromuconate cycloisomerase
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Chloromuconate cycloisomerase oktamer, Rhodococcus opacus
Identifiers
EC no. 5.5.1.7
CAS no. 95990-33-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
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Gene Ontology AmiGO / QuickGO
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NCBI proteins

In enzymology, a chloromuconate cycloisomerase (EC 5.5.1.7) is an enzyme that catalyzes the chemical reaction

2-chloro-2,5-dihydro-5-oxofuran-2-acetate 3-chloro-cis,cis-muconate

Hence, this enzyme has one substrate, 2-chloro-2,5-dihydro-5-oxofuran-2-acetate, and one product, 3-chloro-cis,cis-muconate.

This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is 2-chloro-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). This enzyme is also called muconate cycloisomerase II. This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,4-dichlorobenzene degradation. It employs one cofactor, manganese.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1CHR, 1NU5, and 2CHR.

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<span class="mw-page-title-main">Muconate lactonizing enzyme</span>

Muconate lactonizing enzymes are involved in the breakdown of lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates as a part of the β-ketoadipate pathway in soil microbes. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes. MLEs consist of several strands which have variable reaction favorable parts therefore the configuration of the strands affect its ability to accept protons. The bacterial MLEs belong to the enolase superfamily, several structures from which are known. MLEs have an identifying structure made up of two proteins and two Magnesium ions as well as various classes depending on whether it is bacterial or eukaryotic. The reaction mechanism that MLEs undergo are the reverse of beta-elimination in which the enolate alpha-carbon is protonated. MLEs can undergo mutations caused by a deletion of catB structural genes which can cause some bacteria to lose its functions such as the ability to grow. Additional mutations to MLEs can cause its structure and function to alter and could cause the conformation to change therefore making it an inactive enzyme that is unable to bind its substrate. There is another enzyme called Mandelate Racemase that is very similar to MLEs in the structural way as well as them both being a part of the enolase superfamily. They both have the same end product even though they undergo different chemical reactions in order to reach the end product.

In enzymology, a hydroxyquinol 1,2-dioxygenase (EC 1.13.11.37) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Protocatechuate 3,4-dioxygenase</span>

In enzymology, a protocatechuate 3,4-dioxygenase (EC 1.13.11.3) is an enzyme that catalyzes the chemical reaction

In enzymology, a stizolobate synthase (EC 1.13.11.29) is an enzyme that catalyzes the chemical reaction

In enzymology, a stizolobinate synthase (EC 1.13.11.30) is an enzyme that catalyzes the chemical reaction

In enzymology, a 2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-carboxy-cis,cis-muconate cycloisomerase is an enzyme that catalyzes the chemical reaction

In enzymology, an α-pinene-oxide decyclase is an enzyme that catalyzes the chemical reaction

In enzymology, a carboxy-cis,cis-muconate cyclase is an enzyme that catalyzes the chemical reaction

In enzymology, a dichloromuconate cycloisomerase is an enzyme that catalyzes the chemical reaction

In enzymology, a muconolactone Δ-isomerase is an enzyme that catalyzes the chemical reaction

The enzyme 3-hydroxy-3-isohexenylglutaryl-CoA lyase catalyzes the chemical reaction

The enzyme 4-carboxymuconolactone decarboxylase (EC 4.1.1.44) catalyzes the chemical reaction

<span class="mw-page-title-main">3-dehydroquinate dehydratase</span> Class of enzymes

The enzyme 3-dehydroquinate dehydratase (EC 4.2.1.10) catalyzes the chemical reaction

Cycloisomerase may refer to:

3-Carboxy-<i>cis</i>,<i>cis</i>-muconic acid Chemical compound

3-Carboxy-cis,cis-muconic acid is a metabolite of the catechin degradation by Bradyrhizobium japonicum.

Fumarate lyase belongs to the lyase class of enzymes. These proteins use fumarate as a substrate. They have been shown to share a short conserved sequence around a methionine which is probably involved in the catalytic activity of this type of enzymes.

The biosynthesis of phenylpropanoids involves a number of enzymes.

References