Fenilalanin/tirozinska amonijak-lijaza

Izvor: Wikipedia
Fenilalanin/tirozinska amonijak-lijaza
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 structures

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 \rightleftharpoons trans-cinamat + NH3;;
(2) L-tirozin \rightleftharpoons trans-p-hidroksicinamat + NH3

Ovaj enzim je član familije lijaza aromatičnih aminokiselina.

Reference[uredi - уреди]

  1. 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. 
  2. 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. 
  3. 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. 
  4. 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. 

Literatura[uredi - уреди]

Spoljašnje veze[uredi - уреди]