1215640-72-4

Basic information

• Product Name: 7,13-O,O-diacetyl-2-O-debenzoyl-2-O-propionylbaccatin III
• Synonyms: 7,13-O,O-diacetyl-2-O-debenzoyl-2-O-propionylbaccatin III
• CAS NO: 1215640-72-4
• Molecular Weight: 622.667
• Mol File: 1215640-72-4.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: 7,13-O,O-diacetyl-2-O-debenzoyl-2-O-propionylbaccatin III(CAS DataBase Reference)
• NIST Chemistry Reference: 7,13-O,O-diacetyl-2-O-debenzoyl-2-O-propionylbaccatin III(1215640-72-4)
• EPA Substance Registry System: 7,13-O,O-diacetyl-2-O-debenzoyl-2-O-propionylbaccatin III(1215640-72-4)

Safety Data

• Hazardous Substances Data: 1215640-72-4(Hazardous Substances Data)

Upstream product

• 329318-51-6 7,13-O,O-diacetyl-2-O-debenzoylbaccatin III 
• 317-66-8 S-propionyl-coenzyme-A 

Relevant articles and documents

Point mutations (Q19P and N23K) increase the operational solubility of a 2α-o-benzoyltransferase that conveys various acyl groups from CoA to a taxane acceptor

Two site-directed mutations within the wild-type 2-o-benzoyltransferase (tbf) cDNA, from Taxus cuspidata plants, yielded an encoded protein containing replacement amino acids at Q19P and N23K that map to a solvent-exposed loop region. The likely significant changes in the biophysical, properties invoked by these mutations caused the overexpressed, modified TBT (mTBT) to partition into the soluble enzyme fraction about 5-fold greater than the wild-type enzyme. Sufficient protein could now be acquired to examine the scope of the substrate specificity of mTBT by incubation with 7,13-O,O-diacetyl-2-Odebenzoylbaccatin III that was mixed individually with various substituted benzoyls, alkanoyls, and (E)-butenoyl CoA donors. The mTBT catalyzed the conversion of each 7,13-O,O-diacetyl-2-O-debenzoylbaccatin III to several 7,13-O,O-diacetyl-2O- acyl-2-O-debenzoylbaeeatin III analogues. The relative catalytic efficiency of mTBT with the 7,13-O,O-diacetyl-2-Odebenzoyl surrogate substrate and heterole carbonyl CoA substrates was slightly greater than with the natural aroyl substrate benzoyl CoA, while substituted benzoyl CoA thioesters were less productive. Short-chain hydrocarbon carbonyl and cyclohexanoyl CoA thioesters were also productive, where C4 substrates were transferred by mTBT with ～10- to 17-fold greater catalytic efficiency compared to the transfer of benzoyl. The described broad specificity of mTBT suggests that a plethora of 2-O-acyl variants of the antimitotic paclitaxel can be assembled through biocatalytic sequences.