This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is 3-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing). This enzyme is also called 3-carboxymuconate cyclase. This enzyme participates in benzoate degradation via hydroxylation.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1JOF.
Related Research Articles
The enzyme argininosuccinate lyase (EC 4.3.2.1, ASL, argininosuccinase; systematic name 2-(N ω-L-arginino)succinate arginine-lyase (fumarate-forming)) catalyzes the reversible breakdown of argininosuccinate:
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 2,3-dihydroxybenzoate 2,3-dioxygenase (EC 1.13.11.28) is an enzyme that catalyzes the chemical reaction
In enzymology, a protocatechuate 3,4-dioxygenase (EC 1.13.11.3) 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 chloromuconate cycloisomerase 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 FAD-AMP lyase (cyclizing) catalyzes the reaction
The enzyme 4-carboxymuconolactone decarboxylase (EC 4.1.1.44) catalyzes the chemical reaction
The enzyme 4-hydroxyphenylacetate decarboxylase (EC 4.1.1.83) catalyzes the chemical reaction
The enzyme aconitate decarboxylase (EC 4.1.1.6) catalyzes the chemical reaction
The enzyme gentisate decarboxylase (EC 4.1.1.62) catalyzes the chemical reaction
The enzyme sabinene-hydrate synthase (EC 4.2.3.11) catalyzes the chemical reaction
In enzymology, a hydroxyisourate hydrolase (EC 3.5.2.17) is an enzyme that catalyzes the chemical reaction
Cycloisomerase may refer to:
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.
References
GROSS SR, GAFFORD RD, TATUM EL (1956). "The metabolism of protocatechuic acid by Neurospora". J. Biol. Chem. 219 (2): 781–96. PMID13319299.
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