2-hydroxymuconate tautomerase

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2-hydroxymuconate tautomerase
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EC no. 5.3.2.6
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2-hydroxymuconate tautomerase (EC 5.3.2.6, 4-oxalocrotonate tautomerase, 4-oxalocrotonate isomerase, cnbG (gene), praC (gene), xylH (gene)) is an enzyme with systematic name (2Z,4E)-2-hydroxyhexa-2,4-dienedioate keto-enol isomerase. [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction

(2Z,4E)-2-hydroxyhexa-2,4-dienedioate (3E)-2-oxohex-3-enedioate

Involved in the meta-cleavage pathway for the degradation of phenols, modified phenols and catechols.

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

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">Enol</span> Organic compound with a C=C–OH group

In organic chemistry, alkenols are a type of reactive structure or intermediate in organic chemistry that is represented as an alkene (olefin) with a hydroxyl group attached to one end of the alkene double bond. The terms enol and alkenol are portmanteaus deriving from "-ene"/"alkene" and the "-ol" suffix indicating the hydroxyl group of alcohols, dropping the terminal "-e" of the first term. Generation of enols often involves deprotonation at the α position to the carbonyl group—H+. When this proton is not returned at the end of the stepwise process, the result is an anion termed an enolate. The enolate structures shown are schematic; a more modern representation considers the molecular orbitals that are formed and occupied by electrons in the enolate. Similarly, generation of the enol often is accompanied by "trapping" or masking of the hydroxy group as an ether, such as a silyl enol ether.

3β-Hydroxysteroid dehydrogenase/Δ5-4 isomerase (3β-HSD) is an enzyme that catalyzes the biosynthesis of the steroid progesterone from pregnenolone, 17α-hydroxyprogesterone from 17α-hydroxypregnenolone, and androstenedione from dehydroepiandrosterone (DHEA) in the adrenal gland. It is the only enzyme in the adrenal pathway of corticosteroid synthesis that is not a member of the cytochrome P450 family. It is also present in other steroid-producing tissues, including the ovary, testis and placenta. In humans, there are two 3β-HSD isozymes encoded by the HSD3B1 and HSD3B2 genes.

<span class="mw-page-title-main">Orotidine 5'-phosphate decarboxylase</span>

Orotidine 5'-phosphate decarboxylase or orotidylate decarboxylase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the decarboxylation of orotidine monophosphate (OMP) to form uridine monophosphate (UMP). The function of this enzyme is essential to the de novo biosynthesis of the pyrimidine nucleotides uridine triphosphate, cytidine triphosphate, and thymidine triphosphate. OMP decarboxylase has been a frequent target for scientific investigation because of its demonstrated extreme catalytic efficiency and its usefulness as a selection marker for yeast strain engineering.

<span class="mw-page-title-main">2,4 Dienoyl-CoA reductase</span> Class of enzymes

2,4 Dienoyl-CoA reductase also known as DECR1 is an enzyme which in humans is encoded by the DECR1 gene which resides on chromosome 8. This enzyme catalyzes the following reactions

<span class="mw-page-title-main">4-Oxalocrotonate tautomerase</span>

4-Oxalocrotonate tautomerase or 4-OT is an enzyme that converts 2-hydroxymuconate to the αβ-unsaturated ketone, 2-oxo-3-hexenedioate. This enzyme forms part of a bacterial metabolic pathway that oxidatively catabolizes toluene, o-xylene, 3-ethyltoluene, and 1,2,4-trimethylbenzene into intermediates of the citric acid cycle. With a monomer size of just 62 amino acid residues, the 4-Oxalocrotonate tautomerase is one of the smallest enzyme subunits known. However, in solution, the enzyme forms a hexamer of six identical subunits, so the active site may be formed by amino acid residues from several subunits. This enzyme is also unusual in that it uses a proline residue at the amino terminus as an active site residue.

In enzymology, a manganese peroxidase (EC 1.11.1.13) is an enzyme that catalyzes the chemical reaction

In enzymology, a 5-carboxymethyl-2-hydroxymuconate Delta-isomerase is an enzyme that catalyzes the chemical reaction

In enzymology, an ascopyrone tautomerase is an enzyme that catalyzes the chemical reaction

In enzymology, an oxaloacetate tautomerase is an enzyme that catalyzes the chemical reaction

In enzymology, phenylpyruvate tautomerase or Macrophage migration inhibitory factor is an enzyme that catalyzes the chemical reaction

In enzymology, a 2-hydroxymuconate-semialdehyde hydrolase (EC 3.7.1.9) is an enzyme that catalyzes the chemical reaction

The enzyme dTDP-glucose 4,6-dehydratase (EC 4.2.1.46) catalyzes the chemical reaction

The enzyme methylglyoxal synthase catalyzes the chemical reaction

<span class="mw-page-title-main">ECH1</span> Protein-coding gene in the species Homo sapiens

Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial is an enzyme that in humans is encoded by the ECH1 gene.

2-Hydroxymuconate-6-semialdehyde dehydrogenase (EC 1.2.1.85, xylG [gene], praB [gene] ) is an enzyme with systematic name (2E,4Z)-2-hydroxy-6-oxohexa-2,4-dienoate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

2-hydroxy-6-oxonona-2,4-dienedioate hydrolase (EC 3.7.1.14, mhpC (gene)) is an enzyme with systematic name (2Z,4E)-2-hydroxy-6-oxona-2,4-dienedioate succinylhydrolase. This enzyme catalyses the following chemical reaction:

  1. (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O (2Z)-2-hydroxypenta-2,4-dienoate + succinate
  2. (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate + H2O (2Z)-2-hydroxypenta-2,4-dienoate + fumarate

2-hydroxyhexa-2,4-dienoate hydratase (EC 4.2.1.132, tesE (gene), hsaE (gene)) is an enzyme with systematic name 4-hydroxy-2-oxohexanoate hydro-lyase ((2Z,4Z)-2-hydroxyhexa-2,4-dienoate-forming). This enzyme catalyses the following chemical reaction

2,4,6-Tri-<i>tert</i>-butylphenol Chemical compound

2,4,6-Tri-tert-butylphenol (2,4,6-TTBP) is a phenol symmetrically substituted with three tert-butyl groups and thus strongly sterically hindered. 2,4,6-TTBP is a readily oxidizable aromatic compound and a weak acid. It oxidizes to give the deep-blue 2,4,6-tri-tert-butylphenoxy radical. 2,4,6-TTBP is related to 2,6-di-tert-butylphenol, which is widely used as an antioxidant in industrial applications. These compounds are colorless solids.

References

  1. Whitman CP, Aird BA, Gillespie WR, Stolowich NJ (1991). "Chemical and enzymatic ketonization of 2-hydroxymuconate, a conjugated enol". J. Am. Chem. Soc. 113 (8): 3154–3162. doi:10.1021/ja00008a052.
  2. Whitman CP, Hajipour G, Watson RJ, Johnson WH, Bembenek ME, Stolowich NJ (1992). "Stereospecific ketonization of 2-hydroxymuconate by 4-oxalocrotonate tautomerase and 5-(carboxymethyl)-2-hydroxymuconate isomerase". J. Am. Chem. Soc. 114 (26): 10104–10110. doi:10.1021/ja00052a002.
  3. Subramanya HS, Roper DI, Dauter Z, Dodson EJ, Davies GJ, Wilson KS, Wigley DB (January 1996). "Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases". Biochemistry. 35 (3): 792–802. doi:10.1021/bi951732k. PMID   8547259.
  4. Stivers JT, Abeygunawardana C, Mildvan AS, Hajipour G, Whitman CP, Chen LH (January 1996). "Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: affinity labeling and heteronuclear NMR studies". Biochemistry. 35 (3): 803–13. doi:10.1021/bi951077g. PMID   8547260.
  5. Wang SC, Johnson WH, Czerwinski RM, Stamps SL, Whitman CP (October 2007). "Kinetic and stereochemical analysis of YwhB, a 4-oxalocrotonate tautomerase homologue in Bacillus subtilis: mechanistic implications for the YwhB- and 4-oxalocrotonate tautomerase-catalyzed reactions". Biochemistry. 46 (42): 11919–29. doi:10.1021/bi701231a. PMC   2531070 . PMID   17902707.
  6. Kasai D, Fujinami T, Abe T, Mase K, Katayama Y, Fukuda M, Masai E (November 2009). "Uncovering the protocatechuate 2,3-cleavage pathway genes". Journal of Bacteriology. 191 (21): 6758–68. doi:10.1128/JB.00840-09. PMC   2795304 . PMID   19717587.