Skip to content
Surf Wiki
Save to docs
general/ec-2-3-1

From Surf Wiki (app.surf) — the open knowledge base

Tropine acyltransferase


FieldValue
NameTropine acyltransferase
EC_number2.3.1.185
CAS_number138440-79-6, 162535-29-7

Tropine acyltransferase (, 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. This enzyme catalyses the following chemical reaction

: acyl-CoA + tropine \rightleftharpoons CoA + O-acyltropine

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

References

References

  1. (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.
  2. (1994). "Esterification reactions in the biosynthesis of tropane alkaloids in transformed root cultures". Plant Cell Tissue Organ Cult..
  3. (November 1999). "Specificities of the enzymes of N-alkyltropane biosynthesis in Brugmansia and Datura". Phytochemistry.
  4. (May 2006). "Functional genomic analysis of alkaloid biosynthesis in Hyoscyamus niger reveals a cytochrome P450 involved in littorine rearrangement". Chemistry & Biology.
Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

Want to explore this topic further?

Ask Mako anything about Tropine acyltransferase — get instant answers, deeper analysis, and related topics.

Research with Mako

Free with your Surf account

Content sourced from Wikipedia, available under CC BY-SA 4.0.

This content may have been generated or modified by AI. CloudSurf Software LLC is not responsible for the accuracy, completeness, or reliability of AI-generated content. Always verify important information from primary sources.

Report