Fenilalaninska amonijak-lijaza
| Fenilalaninska amonijak-lijaza | |||||||||
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| Fenilalaninska amonijak-lijaza dimer, Taxus canadensis | |||||||||
| Identifikatori | |||||||||
| EC broj | 4.3.1.24 | ||||||||
| CAS broj | 9024-28-6 | ||||||||
| 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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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 trans-cinamat + NH3
Ovaj enzim je član familije lijaza aromatičnih aminokiselina.
- ↑ Koukol, J. and 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.
- ↑ Young, M.R. and Neish, A.C. (1966). „Properties of the ammonia-lyases deaminating phenylalanine and related compounds in Triticum sestivum and Pteridium aquilinum”. Phytochemistry 5: 1121-1132.
- ↑ 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.
- ↑ 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.
- ↑ Ritter, H. and 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
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