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Butyryl-coenzyme A (or butyryl-CoA) is the coenzyme A-activated form of butyric acid.[1]

Stereo skeletal formula of tetradeprotonated butyryl-coA ({[(2R,3S,4R,5R)-5-yl,-2-meth,-4-hydrox,-3-yl]})
3D model (JSmol)
  • 260 ☑Y
  • 388318 {[(2R,3S,4R,5R)-5-yl,-2-meth,-4-hydrox,-3-yl]} ☑Y
  • 5292369 {[(2R,3R,5R)-5-yl,-2-({[{[(3S)-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]} ☑Y
MeSH butyryl-coenzyme+A
  • 265
  • 25201345 {[(2R,5R)-5-yl,-2-({[{[(3R)-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]}
  • 439173 {[(2R,3S,4R,5R)-5-yl,-2-meth,-4-hydrox,-3-yl]}
  • 46907881 {[(2R,3R,5R)-5-yl,-2-({[{[(3R)-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]}
  • 6917112 {[(2R,3R,5R)-5-yl,-2-({[{[(3S)-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]}
Molar mass 837.62 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references

It is acted upon by butyryl-CoA dehydrogenase.

It is an intermediary compound of ABE fermentation

Butyryl-COA dehydrogenase Oxidation-Reduction reaction consists of 2 electron transfer with 1 proton exchange. Ideally, this will occur between pH 5.5 and 7 for optimal reaction. In this range is where the enzyme is most stable.

From Redox data, Butyryl-COA dehydrogenase shows little to no activity at pH higher than 7.0. This is important as Enzyme midpoint potential is at pH 7.0 and at 25 degrees C. Therefore, changes above from this value will denature the enzyme.[2]


  1. ^ [1]
  2. ^ Berzin, Vel; Tyurin, Michael; Kiriukhin, Michael (2013-01-08). "Selective n-Butanol Production by Clostridium sp. MTButOH1365 During Continuous Synthesis Gas Fermentation Due to Expression of Synthetic Thiolase, 3-Hydroxy Butyryl-CoA Dehydrogenase, Crotonase, Butyryl-CoA Dehydrogenase, Butyraldehyde Dehydrogenase, and NAD-Dependent Butanol Dehydrogenase". Applied Biochemistry and Biotechnology. 169 (3): 950–959. doi:10.1007/s12010-012-0060-7. ISSN 0273-2289. PMID 23292245.