Fenilalanin/tirozinska amonijak-lijaza
Izgled
Fenilalanin/tirozinska amonijak-lijaza | |||||||||
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Identifikatori | |||||||||
EC broj | 4.3.1.25 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Fenilalanin/tirozinska amonijak-lijaza (EC 4.3.1.25, PTAL, bifunkcionalni PAL) je enzim sa sistematskim imenom L-fenilalanin(or L-tirozin):trans-cinamat(or trans-p-hidroksicinamat) amonijak-lijaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) L-fenilalanin trans-cinamat + NH3;;
- (2) L-tirozin trans-p-hidroksicinamat + NH3
Ovaj enzim je član familije lijaza aromatičnih aminokiselina.
- ↑ Rösler, J., Krekel, F., Amrhein, N. and Schmid, J. (1997). „Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity”. Plant Physiol. 113: 175-179. PMID 9008393.
- ↑ Watts, K.T., Mijts, B.N., Lee, P.C., Manning, A.J. and Schmidt-Dannert, C. (2006). „Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family”. Chem. Biol. 13: 1317-1326. PMID 17185227.
- ↑ Louie, G.V., Bowman, M.E., Moffitt, M.C., Baiga, T.J., Moore, B.S. and Noel, J.P. (2006). „Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases”. Chem. Biol. 13: 1327-1338. PMID 17185228.
- ↑ Schwede, T.F., Rétey, J. and Schulz, G.E. (1999). „Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile”. Biochemistry 38: 5355-5361. PMID 10220322.
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