Hydrogen-sulfide S-acetyltransferase

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hydrogen-sulfide S-acetyltransferase
Identifiers
EC no. 2.3.1.10
CAS no. 9029-92-9
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MetaCyc metabolic pathway
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In enzymology, a hydrogen-sulfide S-acetyltransferase (EC 2.3.1.10) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + hydrogen sulfide CoA + thioacetate

Thus, the two substrates of this enzyme are acetyl-CoA and hydrogen sulfide, whereas its two products are CoA and thioacetate.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:hydrogen-sulfide S-acetyltransferase. This enzyme is also called hydrogen-sulfide acetyltransferase.

Related Research Articles

The iron–sulfur world hypothesis is a set of proposals for the origin of life and the early evolution of life advanced in a series of articles between 1988 and 1992 by Günter Wächtershäuser, a Munich patent lawyer with a degree in chemistry, who had been encouraged and supported by philosopher Karl R. Popper to publish his ideas. The hypothesis proposes that early life may have formed on the surface of iron sulfide minerals, hence the name. It was developed by retrodiction from extant biochemistry in conjunction with chemical experiments.

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

Choline acetyltransferase is a transferase enzyme responsible for the synthesis of the neurotransmitter acetylcholine. ChAT catalyzes the transfer of an acetyl group from the coenzyme acetyl-CoA to choline, yielding acetylcholine (ACh). ChAT is found in high concentration in cholinergic neurons, both in the central nervous system (CNS) and peripheral nervous system (PNS). As with most nerve terminal proteins, ChAT is produced in the body of the neuron and is transported to the nerve terminal, where its concentration is highest. Presence of ChAT in a nerve cell classifies this cell as a "cholinergic" neuron. In humans, the choline acetyltransferase enzyme is encoded by the CHAT gene.

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

Chloramphenicol acetyltransferase is a bacterial enzyme that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism.

<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.

Aralkylamine <i>N</i>-acetyltransferase Class of enzymes

Aralkylamine N-acetyltransferase (AANAT), also known as arylalkylamine N-acetyltransferase or serotonin N-acetyltransferase (SNAT), is an enzyme that is involved in the day/night rhythmic production of melatonin, by modification of serotonin. It is in humans encoded by the ~2.5 kb AANAT gene containing four exons, located on chromosome 17q25. The gene is translated into a 23 kDa large enzyme. It is well conserved through evolution and the human form of the protein is 80 percent identical to sheep and rat AANAT. It is an acetyl-CoA-dependent enzyme of the GCN5-related family of N-acetyltransferases (GNATs). It may contribute to multifactorial genetic diseases such as altered behavior in sleep/wake cycle and research is on-going with the aim of developing drugs that regulate AANAT function.

<span class="mw-page-title-main">Acetyl-CoA C-acetyltransferase</span> Class of enzymes

In enzymology, an acetyl-CoA C-acetyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, an aminoglycoside N3'-acetyltransferase (EC 2.3.1.81) is an enzyme that catalyzes the chemical reaction

<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

In enzymology, a cysteine-S-conjugate N-acetyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a deacetylcephalosporin-C acetyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, formate C-acetyltransferase is an enzyme. Pyruvate formate lyase is found in Escherichia coli and other organisms. It helps regulate anaerobic glucose metabolism. Using radical non-redox chemistry, it catalyzes the reversible conversion of pyruvate and coenzyme-A into formate and acetyl-CoA. The reaction occurs as follows:

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

In enzymology, glucosamine-phosphate N-acetyltransferase (GNA) is an enzyme that catalyzes the transfer of an acetyl group from acetyl-CoA to the primary amine in glucosamide-6-phosphate, generating a free CoA and N-acetyl-D-glucosamine-6-phosphate.

In enzymology, a maltose O-acetyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a peptide alpha-N-acetyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a sulfoacetaldehyde acetyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a tetrahydrodipicolinate N-acetyltransferase (EC 2.3.1.89) is an enzyme that catalyzes the chemical reaction

In enzymology, a thioethanolamine S-acetyltransferase 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">Potassium thioacetate</span> Organosulfur compound (CH3COS- K+)

Potassium thioacetate is an organosulfur compound and a salt with the formula CH3COSK+. This white, water-soluble solid is used as a reagent for preparing thioacetate esters and other derivatives.

References