Fenilalaninska amonijak-lijaza

Fenilalaninska amonijak-lijaza
Identifikatori
EC broj	4.3.1.24
CAS broj	9024-28-6
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
Pretraga PMC članci PubMed članci NCBI proteini

Fenilalaninska amonijak-lijaza (EC 4.3.1.24, fenilalaninska deaminaza, fenilalaninska amonijum-lijaza, PAL, L-fenilalaninska amonijak-lijaza, Phe amonijak-lijaza) je enzim sa sistematskim imenom L-fenilalanin amonijak-lijaza (formira trans-cinamat).^{[1][2][3][4][5][6][7][8][9]} Ovaj enzim katalizuje sledeću hemijsku reakciju

L-fenilalanin ${\displaystyle \rightleftharpoons }$ trans-cinamat + NH₃

Ovaj enzim je član familije lijaza aromatičnih aminokiselina.

Reference

1. Koukol, J. & Conn, E.E. (1961). „The metabolism of aromatic compounds in higher plants. IV. Purification and properties of the phenylalanine deaminase of Hordeum vulgare”. J. Biol. Chem. 236: 2692—2698. PMID 14458851. 
2. Young, M.R. & Neish, A.C. (1966). „Properties of the ammonia-lyases deaminating phenylalanine and related compounds in Triticum sestivum and Pteridium aquilinum”. Phytochemistry. 5: 1121—1132. 
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. CS1 одржавање: Вишеструка имена: списак аутора (веза)
4. Calabrese, J.C., Jordan, D.B., Boodhoo, A., Sariaslani, S. and Vannelli, T. (2004). „Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis”. Biochemistry. 43: 11403—11416. PMID 15350127. CS1 одржавање: Вишеструка имена: списак аутора (веза)
5. Ritter, H. & Schulz, G.E. (2004). „Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase”. Plant Cell. 16: 3426—3436. PMID 15548745. 
6. 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. CS1 одржавање: Вишеструка имена: списак аутора (веза)
7. Appert, C., Logemann, E., Hahlbrock, K., Schmid, J. and Amrhein, N. (1994). „Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.)”. Eur. J. Biochem. 225: 491—499. PMID 7925471. CS1 одржавање: Вишеструка имена: списак аутора (веза)
8. Cochrane, F.C., Davin, L.B. and Lewis, N.G. (2004). „The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms”. Phytochemistry. 65: 1557—1564. PMID 15276452. CS1 одржавање: Вишеструка имена: списак аутора (веза)
9. 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. CS1 одржавање: Вишеструка имена: списак аутора (веза)

Literatura

• Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X. 
• Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036. 
• Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0. 
• Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097. 

Spoljašnje veze

• Phenylalanine+ammonia-lyase на US National Library of Medicine Medical Subject Headings (MeSH)