Literature summary for 1.4.3.2 extracted from

Findrik, Z.; Vasic-Racki, E.; Primozic, M.; Habulin, M.; Knez, Z.
Enzymatic activity of L-amino acid oxidase from snake venom Crotalus adamanteus in supercritical CO2 (2005), Biocatal. Biotransform., 23, 315-321.

No PubMed abstract available

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Application

Application	Comment	Organism
synthesis	use of enzyme as a catalyst in supercritical CO2. enzyme activity increases after exposure to supercritical conditions by up to 15%. Enzyme is more stable in supercritical CO2 than under atmospherical pressure, and oxidation of 3,4-dihydroxyphenyl-L-Ala is best under supercritical conditions	Crotalus adamanteus

Organism

Organism	UniProt	Comment	Textmining
Crotalus adamanteus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3,4-dihydroxyphenyl-L-Ala + H2O + O2	-	Crotalus adamanteus	3-(3,4-dihydroxyphenyl)-2-oxopropanoate + NH3 + H2O2	-	?

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Release 2023.1 (January 2023)