Acyl-(acyl-carrier-protein)—UDP-N-acetylglucosamine O-acyltransferase

Last updated
acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase
Identifiers
EC no. 2.3.1.129
CAS no. 105843-69-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, an acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase (EC 2.3.1.129) is an enzyme that catalyzes the chemical reaction

(R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetylglucosamine [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine

Thus, the two substrates of this enzyme are (R)-3-hydroxytetradecanoyl-acyl-carrier-protein and UDP-N-acetylglucosamine, whereas its two products are acyl-carrier-protein and UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine.

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 (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl) transferase. Other names in common use include UDP-N-acetylglucosamine acyltransferase and uridine diphosphoacetylglucosamine acyltransferase. This enzyme participates in lipopolysaccharide biosynthesis.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1J2Z, 1LXA, 2AQ9, 2JF2, 2JF3, 2QIA, and 2QIV.

Related Research Articles

Uridine diphosphate <i>N</i>-acetylglucosamine Chemical compound

Uridine diphosphate N-acetylglucosamine or UDP-GlcNAc is a nucleotide sugar and a coenzyme in metabolism. It is used by glycosyltransferases to transfer N-acetylglucosamine residues to substrates. D-Glucosamine is made naturally in the form of glucosamine-6-phosphate, and is the biochemical precursor of all nitrogen-containing sugars. To be specific, glucosamine-6-phosphate is synthesized from fructose 6-phosphate and glutamine as the first step of the hexosamine biosynthesis pathway. The end-product of this pathway is UDP-GlcNAc, which is then used for making glycosaminoglycans, proteoglycans, and glycolipids.

In enzymology, an acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase 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

In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase I is an enzyme that catalyzes the chemical reaction

In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase II (EC 2.3.1.179) is an enzyme that catalyzes the chemical reaction

In enzymology, a diacylglycerol-sterol O-acyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a galactosylacylglycerol O-acyltransferase is an enzyme that catalyzes the chemical reaction

<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.

<span class="mw-page-title-main">Homocitrate synthase</span> Enzyme

In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction

In enzymology, a lipoyl(octanoyl) transferase (EC 2.3.1.181) is an enzyme that catalyzes the chemical reaction

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

Sterol O-acyltransferase is an intracellular protein located in the endoplasmic reticulum that forms cholesteryl esters from cholesterol.

<span class="mw-page-title-main">UDP-N-acetylglucosamine 1-carboxyvinyltransferase</span> Class of enzymes

In enzymology, an UDP-N-acetylglucosamine 1-carboxyvinyltransferase is an enzyme that catalyzes the first committed step in peptidoglycan biosynthesis of bacteria:

In enzymology, a [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, an UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme that catalyzes the chemical reaction

UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase is an enzyme with systematic name (3R)-3-hydroxymyristoyl-(acyl-carrier protein):UDP-3-O-( -3-hydroxymyristoyl)-alpha-D-glucosamine N-acetyltransferase. This enzyme catalyses the following chemical reaction

Protein <i>O</i>-GlcNAc transferase Protein-coding gene in the species Homo sapiens

Protein O-GlcNAc transferase also known as OGT or O-linked N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the OGT gene. OGT catalyzes the addition of the O-GlcNAc post-translational modification to proteins.

UDP-3-O-acyl-N-acetylglucosamine deacetylase, also known as LpxC, is a zinc-dependent enzyme involved in bacterial lipid A biosynthesis, catalyzing the removal of the acetyl group from UDP-3-O-acyl-N-acetylglucosamine, a key step in the production of lipopolysaccharides in the outer membrane of Gram-negative bacteria.

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

Ghrelin O-acyltransferase also known as membrane bound O-acyltransferase domain containing 4 is an enzyme that in humans is encoded by the MBOAT4 gene. It is homologous to other membrane-bound O-acyltransferases. It is a polytopic membrane protein what takes part in lipid signaling reactions. It is the only known enzyme that catalyzes the acylation of ghrelin through the transfer of n-octanoic acid to ghrelin Ser3. Ghrelin O-acyltransferase function is essential in regulation of appetite and the release of growth hormone. Ghrelin O-acyltransferase is a target for scientific research due to promising applications in the treatment of diabetes, eating disorders, and metabolic diseases.

References