Diaminobutyrate acetyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.3.1.178 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a diaminobutyrate acetyltransferase (EC 2.3.1.178) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are acetyl-CoA and L-2,4-diaminobutanoate, whereas its two products are CoA and N4-acetyl-L-2,4-diaminobutanoate.
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:L-2,4-diaminobutanoate N4-acetyltransferase. Other names in common use include L-2,4-diaminobutyrate acetyltransferase, L-2,4-diaminobutanoate acetyltransferase, EctA, diaminobutyric acid acetyltransferase, DABA acetyltransferase, 2,4-diaminobutanoate acetyltransferase, DAB acetyltransferase, DABAcT, and acetyl-CoA:L-2,4-diaminobutanoate 4-N-acetyltransferase. This enzyme participates in glycine, serine and threonine metabolism.
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.
Ectoine is a natural compound found in several species of bacteria. It is a compatible solute which serves as a protective substance by acting as an osmolyte and thus helps organisms survive extreme osmotic stress. Ectoine is found in high concentrations in halophilic microorganisms and confers resistance towards salt and temperature stress. Ectoine was first identified in the microorganism Ectothiorhodospira halochloris, but has since been found in a wide range of Gram-negative and Gram-positive bacteria. Other species of bacteria in which ectoine was found include:
N-Acetylglutamate synthase (NAGS) is an enzyme that catalyses the production of N-acetylglutamate (NAG) from glutamate and acetyl-CoA.
The enzyme diaminobutyrate decarboxylase (EC 4.1.1.86) catalyzes the chemical reaction
The enzyme ectoine synthase (EC ) catalyzes the chemical reaction
In enzymology, a [acyl-carrier-protein] S-acetyltransferase is an enzyme that catalyzes the reversible chemical reaction
Carnitine O-acetyltransferase also called carnitine acetyltransferase is an enzyme that encoded by the CRAT gene that catalyzes the chemical reaction
In enzymology, a deacetylcephalosporin-C acetyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction
In enzymology, a serine O-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 diaminobutyrate-2-oxoglutarate transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, a diaminobutyrate-pyruvate transaminase is an enzyme that catalyzes the chemical reaction
Heparan-α-glucosaminide N-acetyltransferase is an enzyme that in humans is encoded by the HGSNAT gene.
In molecular biology, members of the ArgJ protein family are bifunctional protein that catalyses the first and fifth steps in arginine biosynthesis. The structure has been determined for glutamate N-acetyltransferase 2, an ArgJ-like protein from Streptomyces clavuligerus.
Acetoin dehydrogenase (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme with systematic name acetyl-CoA:acetoin O-acetyltransferase. This enzyme catalyses the following chemical reaction
UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase is an enzyme with systematic name acetyl-CoA:UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate N-acetyltransferase. This enzyme catalyses the following chemical reaction
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase is an enzyme with systematic name acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase. This enzyme catalyses the following chemical reaction
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase is an enzyme with systematic name UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction
Marinococcus halophilus is a Gram-positive and halophilic bacterium from the genus of Marinococcus which has been isolated from a salted mackerel. Marinococcus halophilus produces ectoine.