Tropine acyltransferase

Last updated
Tropine acyltransferase
Identifiers
EC no. 2.3.1.185
CAS no. 162535-29-7&title= 138440-79-6, 162535-29-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Tropine acyltransferase (EC 2.3.1.185, tropine:acyl-CoA transferase, acetyl-CoA:tropan-3-ol acyltransferase, tropine acetyltransferase, tropine tigloyltransferase, TAT) is an enzyme with systematic name acyl-CoA:tropine O-acyltransferase. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

acyl-CoA + tropine CoA + O-acyltropine

This enzyme exhibits absolute specificity for the endo/3alpha configuration found in tropine as pseudotropine.

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">Tropinone</span> Chemical compound

Tropinone is an alkaloid, famously synthesised in 1917 by Robert Robinson as a synthetic precursor to atropine, a scarce commodity during World War I. Tropinone and the alkaloids cocaine and atropine all share the same tropane core structure. Its corresponding conjugate acid at pH 7.3 major species is known as tropiniumone.

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

Malonyl-CoA is a coenzyme A derivative of malonic acid.

Fatty acid degradation is the process in which fatty acids are broken down into their metabolites, in the end generating acetyl-CoA, the entry molecule for the citric acid cycle, the main energy supply of living organisms, including bacteria and animals. It includes three major steps:

<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.

In enzymology, a tropinone reductase I (EC 1.1.1.206) is an enzyme that catalyzes the chemical reaction

In enzymology, a tropinone reductase II (EC 1.1.1.236) is an enzyme that catalyzes the chemical reaction

In enzymology, a 1-acylglycerol-3-phosphate O-acyltransferase is an enzyme that catalyzes the chemical reaction

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

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

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

Carnitine O-octanoyltransferase is a member of the transferase family, more specifically a carnitine acyltransferase, a type of enzyme which catalyzes the transfer of acyl groups from acyl-CoAs to carnitine, generating CoA and an acyl-carnitine. The systematic name of this enzyme is octanoyl-CoA:L-carnitine O-octanoyltransferase. Other names in common use include medium-chain/long-chain carnitine acyltransferase, carnitine medium-chain acyltransferase, easily solubilized mitochondrial carnitine palmitoyltransferase, and overt mitochondrial carnitine palmitoyltransferase. Specifically, CROT catalyzes the chemical reaction:

<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

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

In molecular biology, hydroxymethylglutaryl-CoA synthase or HMG-CoA synthase EC 2.3.3.10 is an enzyme which catalyzes the reaction in which acetyl-CoA condenses with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). This reaction comprises the second step in the mevalonate-dependent isoprenoid biosynthesis pathway. HMG-CoA is an intermediate in both cholesterol synthesis and ketogenesis. This reaction is overactivated in patients with diabetes mellitus type 1 if left untreated, due to prolonged insulin deficiency and the exhaustion of substrates for gluconeogenesis and the TCA cycle, notably oxaloacetate. This results in shunting of excess acetyl-CoA into the ketone synthesis pathway via HMG-CoA, leading to the development of diabetic ketoacidosis.

In enzymology, a salutaridinol 7-O-acetyltransferase 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.

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

Pseudotropine acyltransferase is an enzyme with systematic name acyl-CoA:pseudotropine O-acyltransferase. This enzyme catalyses the following 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

<i>O</i>-Acylpseudotropine Class of chemical compounds

An O-acylpseudotropine is any derivative of pseudotropine in which the alcohol group is substituted with an acyl group.

References

  1. Robins RJ, Bachmann P, Robinson T, Rhodes MJ, Yamada Y (November 1991). "The formation of 3 alpha- and 3 beta-acetoxytropanes by Datura stramonium transformed root cultures involves two acetyl-CoA-dependent acyltransferases". FEBS Letters. 292 (1–2): 293–7. doi: 10.1016/0014-5793(91)80887-9 . PMID   1959620.
  2. Robins, R.J.; Bachmann,P.; Peerless, A.C.J.; Rabot, S. (1994). "Esterification reactions in the biosynthesis of tropane alkaloids in transformed root cultures". Plant Cell Tissue Organ Cult. 38: 241–247. doi:10.1007/bf00033883.
  3. Boswell HD, Dräger B, McLauchlan WR, Portsteffen A, Robins DJ, Robins RJ, Walton NJ (November 1999). "Specificities of the enzymes of N-alkyltropane biosynthesis in Brugmansia and Datura". Phytochemistry. 52 (5): 871–8. doi:10.1016/S0031-9422(99)00293-9. PMID   10626376.
  4. Li R, Reed DW, Liu E, Nowak J, Pelcher LE, Page JE, Covello PS (May 2006). "Functional genomic analysis of alkaloid biosynthesis in Hyoscyamus niger reveals a cytochrome P450 involved in littorine rearrangement". Chemistry & Biology. 13 (5): 513–20. doi: 10.1016/j.chembiol.2006.03.005 . PMID   16720272.