Butyryl-CoA

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

Butyryl-CoA
Stereo skeletal formula of tetradeprotonated butyryl-coA ({[(2R,3S,4R,5R)-5-yl,-2-meth,-4-hydrox,-3-yl]})
Names
Preferred IUPAC name
[(2R,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methyl (3R)-4-[(3-{[2-(butanoylsulfanyl)ethyl]amino}-3-oxopropyl)amino]-3-hydroxy-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate
Identifiers
3D model (JSmol)
3DMet
ChEBI
ChemSpider
  • 260 checkY
  • 388318 {[(2R,3S,4R,5R)-5-yl,-2-meth,-4-hydrox,-3-yl]} checkY
  • 5292369 {[(2R,3R,5R)-5-yl,-2-({[{[(3S)-3-hydrox]-ox}-phosph]-ox}-meth),-3-yl]} checkY
KEGG
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]}
  • InChI=1S/C25H42N7O17P3S/c1-4-5-16(34)53-9-8-27-15(33)6-7-28-23(37)20(36)25(2,3)11-46-52(43,44)49-51(41,42)45-10-14-19(48-50(38,39)40)18(35)24(47-14)32-13-31-17-21(26)29-12-30-22(17)32/h12-14,18-20,24,35-36H,4-11H2,1-3H3,(H,27,33)(H,28,37)(H,41,42)(H,43,44)(H2,26,29,30)(H2,38,39,40) checkY
    Key: CRFNGMNYKDXRTN-UHFFFAOYSA-N checkY
  • CCCC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12
Properties
C25H42N7O17P3S
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 is also converted from Crotonyl-CoA. This occurs when FADH- transfers a hydride to crotonyl-CoA.[2] It is essential in reducing ferredoxins in anaerobic bacteria and archaea so that electron transport phosphorylation and substrate level phosphorylation can occur with increased efficiency.[3]

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.[4]

See alsoEdit

ReferencesEdit

  1. ^ [1]
  2. ^ Chowdury, Nilanjan Pal; Mowafy, Amr M.; Demmer, Julius, K.; Upadhyay, Vikrant; Koelzer, Sebastian; Jayamani, Elamparithi; Kahnt, Joerg; Hornung, Marco; Demler; Ermler; Buckel. "Studies on the Mechanism of Electron Bifurcation Catalyzed by Electron Transferring Flavoprotein (Etf) and Butyryl-CoA Dehydrogenase (Bcd) of Acidaminococcus Fermentans". Journal of Biological Chemistry. 289 (8): 5145–5157. doi:10.1074/jbc.M113.521013. PMC 3931072.
  3. ^ Demmer, Julius K.; Chowdhury, Nilanjan Pal; Selmer, Thorsten; Ermler, Ulrich; Buckel, Wolfgang (2017-11-17). "The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile". Nature Communications. 8 (1): 1577. doi:10.1038/s41467-017-01746-3. PMC 5691135.
  4. ^ 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. S2CID 22534861.