Entry |
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Name |
phenylalanine ammonia-lyase;
phenylalanine deaminase;
phenylalanine ammonium-lyase;
PAL;
L-phenylalanine ammonia-lyase;
Phe ammonia-lyase
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Class |
Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases
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Sysname |
L-phenylalanine ammonia-lyase (trans-cinnamate-forming)
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Reaction(IUBMB) |
L-phenylalanine = trans-cinnamate + NH3 [RN: R00697]
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Reaction(KEGG) |
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Substrate |
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Product |
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Comment |
This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase) and EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family [3]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [9]. The enzyme from some species is highly specific for phenylalanine [7,8].
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History |
EC 4.3.1.24 created 2008 (EC 4.3.1.5 created 1965, part-incorporated 2008)
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Pathway |
ec00940 | Phenylpropanoid biosynthesis |
ec01110 | Biosynthesis of secondary metabolites |
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Orthology |
K10775 | phenylalanine ammonia-lyase |
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Genes |
» show all
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Reference |
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Authors |
KOUKOL J, CONN EE. |
Title |
The metabolism of aromatic compounds in higher plans. IV. Purification and properties of the phenylalanine deaminase of Hordeum vulgare. |
Journal |
J Biol Chem 236:2692-8 (1961) |
Reference |
2 |
Authors |
Young, M.R. and Neish, A.C. |
Title |
Properties of the ammonia-lyases deaminating phenylalanine and related compounds in Triticum sestivum and Pteridium aquilinum. |
Journal |
Phytochemistry 5:1121-1132 (1966) |
Reference |
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Authors |
Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP. |
Title |
Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases. |
Journal |
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Reference |
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Authors |
Calabrese JC, Jordan DB, Boodhoo A, Sariaslani S, Vannelli T. |
Title |
Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis. |
Journal |
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Reference |
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Authors |
Ritter H, Schulz GE |
Title |
Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase. |
Journal |
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Sequence |
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Reference |
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Authors |
Watts KT, Mijts BN, Lee PC, Manning AJ, Schmidt-Dannert C |
Title |
Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family. |
Journal |
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Sequence |
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Reference |
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Authors |
Appert C, Logemann E, Hahlbrock K, Schmid J, Amrhein N |
Title |
Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.). |
Journal |
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Sequence |
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Reference |
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Authors |
Cochrane FC, Davin LB, Lewis NG |
Title |
The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms. |
Journal |
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Sequence |
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Reference |
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Authors |
Schwede TF, Retey J, Schulz GE |
Title |
Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. |
Journal |
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Other DBs |
ExplorEnz - The Enzyme Database: | 4.3.1.24 |
ExPASy - ENZYME nomenclature database: | 4.3.1.24 |
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