IL4I1:FAD oxidises L-Phe to kPPV

Stable Identifier
R-HSA-2160492
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
phenylalanine + H2O + O2 => phenylpyruvate + NH3 + H2O2
Locations in the PathwayBrowser
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Extracellular L-amino-acid oxidase (IL4I1) catalyzes the reaction of phenylalanine, water, and molecular oxygen to form keto-phenylpyruvate, ammonia, and hydrogen peroxide. IL4I1, inferred to form a complex with FAD, has L-amino acid oxidase activity and with a strong preference for phenylalanine. The enzyme, found both in lysosomes and secreted into the extracellular space, is produced in the body by myeloid and dedritic cells (Boulland et al. 2007).

Literature References
PubMed ID Title Journal Year
17356132 Human IL4I1 is a secreted L-phenylalanine oxidase expressed by mature dendritic cells that inhibits T-lymphocyte proliferation

Boulland, ML, Marquet, J, Molinier-Frenkel, V, Moller, P, Guiter, C, Lasoudris, F, Copie-Bergman, C, Baia, M, Gaulard, P, Leroy, K, Castellano, F

Blood 2007
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
L-amino-acid oxidase activity of IL4I1:FAD [extracellular region]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created