propionyl-CoA

Base Information

• Chemical Name: propionyl-CoA
• CAS No.: 317-66-8
• Molecular Formula: C24H40 N7 O17 P3 S
• Molecular Weight: 823.606
• European Community (EC) Number: 206-266-6
• UNII: H7HQA57V5H
• DSSTox Substance ID: DTXSID10185594
• Nikkaji Number: J1.695.704F
• Wikipedia: Propionyl-CoA
• Wikidata: Q2640914
• Metabolomics Workbench ID: 50150
• Mol file: 317-66-8.mol

Synonyms:coenzyme A, propionyl-;propionyl-CoA;propionyl-coenzyme A;propionyl-coenzyme A, 3H-labeled

Chemical Property of propionyl-CoA

Chemical Property:

• Density: 1.86g/cm³
• XLogP3: -5.1
• Hydrogen Bond Donor Count: 9
• Hydrogen Bond Acceptor Count: 22
• Rotatable Bond Count: 21
• Exact Mass: 823.14142500
• Heavy Atom Count: 52
• Complexity: 1400

Purity/Quality:

99% ^*data from raw suppliers

Safty Information:

• Pictogram(s):  
• Hazard Codes: 

MSDS Files:

SDS file from LookChem

Useful:

• Canonical SMILES: CCC(=O)SCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)N2C=NC3=C(N=CN=C32)N)O)OP(=O)(O)O)O
• Isomeric SMILES: CCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=O)(O)OP(=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)N2C=NC3=C(N=CN=C32)N)O)OP(=O)(O)O)O

Technology Process of propionyl-CoA

There total 7 articles about propionyl-CoA which guide to synthetic route it. The literature collected by LookChem mainly comes from the sharing of users and the free literature resources found by Internet computing technology. We keep the original model of the professional version of literature to make it easier and faster for users to retrieve and use. At the same time, we analyze and calculate the most feasible synthesis route with the highest yield for your reference as below:

synthetic route:

Reference yield:

propionic acid anhydride (123-62-6) + coenzyme A (85-61-0) → S-propionyl-coenzyme-A (317-66-8)

Guidance literature:

Reference yield:

succinyl-coenzyme A (604-98-8) → S-propionyl-coenzyme-A (317-66-8)

Guidance literature:

Multi-step reaction with 2 steps

1: Acetobacter aceti succinyl-CoA:acetate CoA transferase C-terminal hexahistidine-tagged / aq. buffer / pH 8 / Enzymatic reaction

2: Acetobacter aceti succinyl-CoA:acetate CoA transferase C-terminal hexahistidine-tagged / aq. buffer / pH 8 / Enzymatic reaction

With Acetobacter aceti succinyl-CoA:acetate CoA transferase C-terminal hexahistidine-tagged; In aq. buffer;

DOI:10.1021/bi300957f

Reference yield:

coenzyme A (85-61-0) → S-propionyl-coenzyme-A (317-66-8)

Guidance literature:

With acetyl-coa-synthetase; ATP;

upstream raw materials:

propionic acid anhydride

coenzyme A

propionic acid

acetylcoenzyme A

Downstream raw materials:

7,13-O,O-diacetyl-2-O-debenzoyl-2-O-propionylbaccatin III

C₂₆H₅₀N₆O₁₄

C₂₆H₅₀N₆O₁₄

urauchimycin B

Refernces

Expanding the chemical space of polyketides through structure-guided mutagenesis of Vitis vinifera stilbene synthase

10.1016/j.biochi.2015.05.019

This research focuses on expanding the chemical space of polyketides, a class of compounds with significant pharmaceutical properties, by employing structure-guided mutagenesis of Vitis vinifera stilbene synthase (VvSTS), a type III polyketide synthase (PKS). The purpose of the study was to diversify the chemical space of polyketides by creating mutants of VvSTS and challenging them with non-natural substrates. The researchers were able to generate 15 previously unreported polyketide molecules by exploring the substrate promiscuity of the wild-type enzyme and all mutants using unnatural substrates. The chemicals used in the process included various non-natural substrates such as propionyl-CoA, myristoyl-CoA, octanoyl-CoA, and methylmalonyl-CoA, which were combined with malonyl-CoA as the extender substrate. The study concluded that by altering the size of the substrate binding pocket and the cyclization pocket through mutations, the researchers could significantly diversify the polyketide space, establishing VvSTS as a candidate enzyme for future protein engineering efforts and as a tool for generating libraries of novel polyketides with potential therapeutic value.