Fatty acid photodecarboxylase (FAP) is an enzyme able to decarboxylate saturated and unsaturated free fatty acids into alkane and alkene respectively (carbon dioxide being the co-product).[1] FAP uses continuous blue light to catalyze decarboxylation, making it a photoenzyme (the third well described). The photoenzyme FAP has been initially discovered in the chloroplast membrane of a microalgae called Chlorella variabilis NC64A; The enzyme was also shown to be well conserved in microalgae in general. Others photoenzymes examples include flavin‐dependent DNA‐repair enzyme and protochlorophyllide oxidoreductases.[2]
Structureedit
The crystallized structure of FAP shows a hydrophobic tunnel consisting of three domains. The inner FAP binding site is flanked by the domain loops that protect it from interacting with solvent. The C-terminal regulates interactions with other proteins and the N-terminal residues on the helical end stabilizes the neighboring tricyclic ring FAD cofactor.[2]
Functionedit
Flavin adenine dinucleotide (FAD) is found to be responsible for capturing light photons that drive the reaction, with the overall FAP efficiency being dependent on both its enzyme concentration and the light intensity.[3] Experimental studies show photon excited FAD react most favorably under continuous blue light (400-520 nm) which produce carbon dioxide from the hydrolysis of fatty acid chains.[3]
FAP's catalytic activity is proportional to the length of the fatty acid chain due to the number of hydrophobic chains present in the hydrophobic tunnel that stabilize substrates.[4] FAP preference to long-chain fatty acid produces higher turnover rate for hydrocarbons, which can then, in principle, be produced as biofuel as a favored alternative.[2]
Referencesedit
^"A Newly Identified Photoenzyme Helps Algae Pump Out Fuel". The Scientist Magazine®. Retrieved 2020-12-04.
^ abHuijbers MM, Zhang W, Tonin F, Hollmann F (October 2018). "Light-Driven Enzymatic Decarboxylation of Fatty Acids". Angewandte Chemie. 57 (41): 13648–13651. doi:10.1002/anie.201807119. PMC6197046. PMID 30106504.
^Zhang W, Ma M, Huijbers MM, Filonenko GA, Pidko EA, van Schie M, et al. (February 2019). "Hydrocarbon Synthesis via Photoenzymatic Decarboxylation of Carboxylic Acids". Journal of the American Chemical Society. 141 (7): 3116–3120. doi:10.1021/jacs.8b12282. PMC6385076. PMID 30673222.
This enzyme-related article is a stub. You can help Wikipedia by expanding it.
fatty, acid, photodecarboxylase, enzyme, able, decarboxylate, saturated, unsaturated, free, fatty, acids, into, alkane, alkene, respectively, carbon, dioxide, being, product, uses, continuous, blue, light, catalyze, decarboxylation, making, photoenzyme, third,. Fatty acid photodecarboxylase FAP is an enzyme able to decarboxylate saturated and unsaturated free fatty acids into alkane and alkene respectively carbon dioxide being the co product 1 FAP uses continuous blue light to catalyze decarboxylation making it a photoenzyme the third well described The photoenzyme FAP has been initially discovered in the chloroplast membrane of a microalgae called Chlorella variabilis NC64A The enzyme was also shown to be well conserved in microalgae in general Others photoenzymes examples include flavin dependent DNA repair enzyme and protochlorophyllide oxidoreductases 2 Structure editThe crystallized structure of FAP shows a hydrophobic tunnel consisting of three domains The inner FAP binding site is flanked by the domain loops that protect it from interacting with solvent The C terminal regulates interactions with other proteins and the N terminal residues on the helical end stabilizes the neighboring tricyclic ring FAD cofactor 2 Function editFlavin adenine dinucleotide FAD is found to be responsible for capturing light photons that drive the reaction with the overall FAP efficiency being dependent on both its enzyme concentration and the light intensity 3 Experimental studies show photon excited FAD react most favorably under continuous blue light 400 520 nm which produce carbon dioxide from the hydrolysis of fatty acid chains 3 FAP s catalytic activity is proportional to the length of the fatty acid chain due to the number of hydrophobic chains present in the hydrophobic tunnel that stabilize substrates 4 FAP preference to long chain fatty acid produces higher turnover rate for hydrocarbons which can then in principle be produced as biofuel as a favored alternative 2 References edit A Newly Identified Photoenzyme Helps Algae Pump Out Fuel The Scientist Magazine Retrieved 2020 12 04 a b c Sorigue D Legeret B Cuine S Blangy S Moulin S Billon E et al September 2017 An algal photoenzyme converts fatty acids to hydrocarbons Science 357 6354 903 907 doi 10 1126 science aan6349 PMID 28860382 a b Huijbers MM Zhang W Tonin F Hollmann F October 2018 Light Driven Enzymatic Decarboxylation of Fatty Acids Angewandte Chemie 57 41 13648 13651 doi 10 1002 anie 201807119 PMC 6197046 PMID 30106504 Zhang W Ma M Huijbers MM Filonenko GA Pidko EA van Schie M et al February 2019 Hydrocarbon Synthesis via Photoenzymatic Decarboxylation of Carboxylic Acids Journal of the American Chemical Society 141 7 3116 3120 doi 10 1021 jacs 8b12282 PMC 6385076 PMID 30673222 nbsp This enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Fatty acid photodecarboxylase amp oldid 1220920129, wikipedia, wiki, book, books, library,
