Mycothiol synthase

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Mycothiol synthase
Identifiers
EC no. 2.3.1.189
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Mycothiol synthase (EC 2.3.1.189, MshD) is an enzyme with systematic name acetyl-CoA:desacetylmycothiol O-acetyltransferase. [1] [2] [3] This enzyme catalyses the following chemical reaction

desacetylmycothiol + acetyl-CoA CoA + mycothiol

This enzyme catalyses the last step in the biosynthesis of mycothiol

Related Research Articles

In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.

<span class="mw-page-title-main">N-acetyltransferase</span>

N-acetyltransferase (NAT) is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to arylamines, arylhydroxylamines and arylhydrazines. They have wide specificity for aromatic amines, particularly serotonin, and can also catalyze acetyl transfer between arylamines without CoA. N-acetyltransferases are cytosolic enzymes found in the liver and many tissues of most mammalian species, except the dog and fox, which cannot acetylate xenobiotics.

<i>N</i>-Acetylglutamate synthase Class of enzymes

N-Acetylglutamate synthase (NAGS) is an enzyme that catalyses the production of N-acetylglutamate (NAG) from glutamate and acetyl-CoA.

<span class="mw-page-title-main">Thiolase</span> Enzymes

Thiolases, also known as acetyl-coenzyme A acetyltransferases (ACAT), are enzymes which convert two units of acetyl-CoA to acetoacetyl CoA in the mevalonate pathway.

<span class="mw-page-title-main">Transsulfuration pathway</span>

The transsulfuration pathway is a metabolic pathway involving the interconversion of cysteine and homocysteine through the intermediate cystathionine. Two transsulfurylation pathways are known: the forward and the reverse.

In enzymology, a mycothiol-dependent formaldehyde dehydrogenase (EC 1.1.1.306) is an enzyme that catalyzes the chemical reaction

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

Isocitrate lyase, or ICL, is an enzyme in the glyoxylate cycle that catalyzes the cleavage of isocitrate to succinate and glyoxylate. Together with malate synthase, it bypasses the two decarboxylation steps of the tricarboxylic acid cycle and is used by bacteria, fungi, and plants.

In enzymology, a 2-isopropylmalate synthase (EC 2.3.3.13) is an enzyme that catalyzes the chemical reaction

In enzymology, a [acyl-carrier-protein] S-acetyltransferase is an enzyme that catalyzes the reversible chemical reaction

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

ATP citrate synthase (also ATP citrate lyase (ACLY)) is an enzyme that in animals represents an important step in fatty acid biosynthesis. By converting citrate to acetyl-CoA, the enzyme links carbohydrate metabolism, which yields citrate as an intermediate, with fatty acid biosynthesis, which consumes acetyl-CoA. In plants, ATP citrate lyase generates cytosolic acetyl-CoA precursors of thousands of specialized metabolites, including waxes, sterols, and polyketides.

<span class="mw-page-title-main">Carnitine O-acetyltransferase</span> Enzyme

Carnitine O-acetyltransferase also called carnitine acetyltransferase is an enzyme that encoded by the CRAT gene that catalyzes the chemical reaction

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

In enzymology, a malate synthase (EC 2.3.3.9) is an enzyme that catalyzes the chemical reaction

In enzymology, a cysteine synthase is an enzyme that catalyzes the chemical reaction

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

Heparan-α-glucosaminide N-acetyltransferase is an enzyme that in humans is encoded by the HGSNAT gene.

<span class="mw-page-title-main">Mycothiol</span> Chemical compound

Mycothiol is an unusual thiol compound found in the Actinomycetota. It is composed of a cysteine residue with an acetylated amino group linked to glucosamine, which is then linked to inositol. The oxidized, disulfide form of mycothiol (MSSM) is called mycothione, and is reduced to mycothiol by the flavoprotein mycothione reductase. Mycothiol biosynthesis and mycothiol-dependent enzymes such as mycothiol-dependent formaldehyde dehydrogenase and mycothione reductase have been proposed to be good drug targets for the development of treatments for tuberculosis.

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

In molecular biology, the citrate synthase family of proteins includes the enzymes citrate synthase EC 2.3.3.1, and the related enzymes 2-methylcitrate synthase EC 2.3.3.5 and ATP citrate lyase EC 2.3.3.8.

<span class="mw-page-title-main">Phosphinothricin acetyltransferase</span>

Phosphinothricin acetyltransferase is an enzyme with systematic name acetyl-CoA:phosphinothricin N-acetyltransferase. This enzyme catalyses the following chemical reaction

D-inositol-3-phosphate glycosyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:1D-myo-inositol 3-phosphate alpha-D-glycosyltransferase. This enzyme catalyses the following chemical reaction

N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (EC 3.5.1.103, MshB) is an enzyme with systematic name 1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol acetylhydrolase. This enzyme catalyses the following chemical reaction

L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase is an enzyme with systematic name L-cysteine:1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol ligase (AMP-forming). This enzyme catalyses the following chemical reaction

References

  1. Spies HS, Steenkamp DJ (August 1994). "Thiols of intracellular pathogens. Identification of ovothiol A in Leishmania donovani and structural analysis of a novel thiol from Mycobacterium bovis". European Journal of Biochemistry. 224 (1): 203–13. doi:10.1111/j.1432-1033.1994.tb20013.x. PMID   8076641.
  2. Koledin T, Newton GL, Fahey RC (November 2002). "Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes". Archives of Microbiology. 178 (5): 331–7. doi:10.1007/s00203-002-0462-y. PMID   12375100.
  3. Vetting MW, Roderick SL, Yu M, Blanchard JS (September 2003). "Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases". Protein Science. 12 (9): 1954–9. doi:10.1110/ps.03153703. PMC   2323992 . PMID   12930994.