Literature summary for 4.3.1.24 extracted from

Maldonado, R.; Goni, O.; Escribano, M.I.; Merodio, C.
Regulation of phenylalanine ammonia-lyase enzyme in Annona fruit: kinetic characteristics and inhibitory effect of ammonia (2007), J. Food Biochem., 31, 161-178.

Search for more literature for 4.3.1.24

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.028	-	L-phenylalanine	enzyme from fruit ripened at low temperature, first Km value using low substrate concentrations, pH 8.8, 30°C	Annona cherimola
0.04	-	L-phenylalanine	enzyme from fruit ripened at room temperature, pH 8.8, 30°C	Annona cherimola
0.049	-	L-phenylalanine	enzyme from fruit ripened in 20% CO2 atmosphere, first Km value using low substrate concentrations, pH 8.8, 30°C	Annona cherimola
0.112	-	L-phenylalanine	enzyme from fruit ripened in 20% CO2 atmosphere, second Km value using high substrate concentrations, pH 8.8, 30°C	Annona cherimola
0.164	-	L-phenylalanine	enzyme from fruit ripened at low temperature, second Km value using low substrate concentrations, pH 8.8, 30°C	Annona cherimola

Organism

Organism	UniProt	Comment	Textmining
Annona cherimola	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Annona cherimola

Source Tissue

Source Tissue	Comment	Organism	Textmining
fruit	-	Annona cherimola	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-phenylalanine	-	Annona cherimola	(E)-cinnamate + NH3	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)