2-methylcitrate dehydratase (2-methyl-trans-aconitate forming)

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2-methylcitrate dehydratase (2-methyl-trans-aconitate forming)
Identifiers
EC no. 4.2.1.117
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2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) (EC 4.2.1.117) is an enzyme with systematic name (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase (2-methyl-trans-aconitate forming). [1] This enzyme catalyses the following chemical reaction

(2S,3S)-2-methylcitrate 2-methyl-trans-aconitate + H2O

Related Research Articles

<span class="mw-page-title-main">Threonine</span> Amino acid

Threonine is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group, a carboxyl group, and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Threonine is synthesized from aspartate in bacteria such as E. coli. It is encoded by all the codons starting AC.

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

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Propionyl-CoA is a coenzyme A derivative of propionic acid. It is composed of a 24 total carbon chain and its production and metabolic fate depend on which organism it is present in. Several different pathways can lead to its production, such as through the catabolism of specific amino acids or the oxidation of odd-chain fatty acids. It later can be broken down by propionyl-CoA carboxylase or through the methylcitrate cycle. In different organisms, however, propionyl-CoA can be sequestered into controlled regions, to alleviate its potential toxicity through accumulation. Genetic deficiencies regarding the production and breakdown of propionyl-CoA also have great clinical and human significance.

In enzymology, a 3-hydroxy-2-methylbutyryl-CoA dehydrogenase (EC 1.1.1.178) is an enzyme that catalyzes the chemical reaction

In enzymology, a trans-aconitate 2-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a trans-aconitate 3-methyltransferase is an enzyme that catalyzes the chemical reaction

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

<span class="mw-page-title-main">Methylisocitrate lyase</span>

The enzyme methylisocitrate lyase catalyzes the chemical reaction

The enzyme 2-methylcitrate dehydratase (EC 4.2.1.79) catalyzes the chemical reaction

The enzyme 2-methylisocitrate dehydratase (EC 4.2.1.99) catalyzes the chemical reaction

In enzymology, a citrate dehydratase (EC 4.2.1.4) is an enzyme that catalyzes the chemical reaction

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The enzyme ectoine synthase (EC ) catalyzes the chemical reaction

In enzymology, a 2-methylcitrate synthase (EC 2.3.3.5) is an enzyme that catalyzes the chemical reaction

Decylcitrate synthase (EC 2.3.3.2) is an enzyme that catalyzes the chemical reaction in enzymology.

3-Isopropylmalate dehydrogenase (EC 1.1.1.85) is an enzyme that is a part of the isopropylmalate dehydrogenase family, which catalyzes the chemical reactions:

<span class="mw-page-title-main">Citrate synthase family</span>

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<span class="mw-page-title-main">Dihydrodipicolinate synthase</span> Class of enzymes

4-Hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7, dihydrodipicolinate synthase, dihydropicolinate synthetase, dihydrodipicolinic acid synthase, L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing), dapA (gene)) is an enzyme with the systematic name L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming). This enzyme catalyses the following chemical reaction

References

  1. Grimek TL, Escalante-Semerena JC (January 2004). "The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo". Journal of Bacteriology. 186 (2): 454–62. doi:10.1128/jb.186.2.454-462.2004. PMC   305763 . PMID   14702315.