41 by: Piper Conner

Student – Piper Conner

Name of enzyme: Biotin—[Acetyl-CoA-carboxylase] ligase

Enzyme Commission number: 6.3.4.15

Where is the enzyme found? Biotin—[Acetyl-Coa-carboxylase] ligase is found primarily in bacteria and plants. It can be found in the cytoplasm and plastids of eukaryotes where its role is in the biosynthesis of fatty acids (O’brien & Young, 2011)

What does the enzyme do? Biotin—[Acetyl-CoA-carboxylase] ligase catalyzses the ligation of biotin to the acetyl-CoA carboxylase. In other words, the enzyme helps attach a small molecule called biotin to a protein called acetyl-CoA carboxylase using ATP as a substrate to provide enough energy for the attachment. This is essential as the acetyl-CoA carboxylase needs biotin to function properly. It is a key step in the fatty acid biosynthesis pathway (Ghosh, 2018). The main job of acetyl-CoA carboxylase is to convert acetyl-CoA into malonyl-CoA.

Any other interesting facts or important information on your enzyme? Biotin—[Acetyl-CoA-carboxylase] ligase activity is dependent on the presence of biotin which serves as a cofactor (Schaefer, 2014). The cofactor covalently attaches to the carboxylase but does not convert into a product at all.

References:

Cronan, J. E. (2023). Biotin protein ligase as you like it: either extraordinarily specific or promiscuous protein biotinylation. Proteins: Structure, Function, and Bioinformatics, 92(4), 435-448. https://doi.org/10.1002/prot.26642

Daniels, K. G. and Beckett, D. (2010). Biochemical properties and biological function of a monofunctional microbial biotin protein ligase. Biochemistry, 49(25), 5358-5365. https://doi.org/10.1021/bi1003958

European Bioinformatics Institute. (n.d.). Biotin—[Acetyl-CoA-carboxylase] ligase. Retrieved October 13, 2024, from https://www.ebi.ac.uk/thornton-srv/m-csa/entry/538/

O’Brien, J. M., & Young, J. D. (2011). “Biotin as a cofactor for enzymatic carboxylation reactions.” Journal of Biological Chemistry.

Schaefer, H. (2014). “Enzymatic functions and biochemistry of biotinylated proteins.” Biochimica et Biophysica Acta.

Tron, C., McNae, I., Nutley, M., Clarke, D. J., Cooper, A., Walkinshaw, M. D., … & Campopiano, D. J. (2009). Structural and functional studies of the biotin protein ligase from aquifex aeolicus reveal a critical role for a conserved residue in target specificity. Journal of Molecular Biology, 387(1), 129-146. https://doi.org/10.1016/j.jmb.2008.12.086

Ghosh, D. (2018). “Fatty Acid Synthesis: Biotin’s Role in Acetyl-CoA Carboxylation.” Annual Review of Biochemistry.

Cronan, J. E. (2023). Biotin protein ligase as you like it: either extraordinarily specific or promiscuous protein biotinylation. Proteins: Structure, Function, and Bioinformatics, 92(4), 435-448. https://doi.org/10.1002/prot.26642