Entry |
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Name |
tyrosine ammonia-lyase;
TAL;
tyrase;
L-tyrosine ammonia-lyase
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Class |
Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases
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Sysname |
L-tyrosine ammonia-lyase (trans-p-hydroxycinnamate-forming)
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Reaction(IUBMB) |
L-tyrosine = trans-p-hydroxycinnamate + NH3 [RN: R00737]
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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), EC 4.3.1.24 (phenylalanine 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 [1]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [3]. The enzyme is far more active with tyrosine than with phenylalanine as substrate, but the substrate specificity can be switched by mutation of a single amino acid (H89F) in the enzyme from the bacterium Rhodobacter sphaeroides [1,2].
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History |
EC 4.3.1.23 created 2008 (EC 4.3.1.5 created 1965, part-incorporated 2008)
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Pathway |
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Orthology |
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Genes |
» show all
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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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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 |
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: | 4.3.1.23 |
ExPASy - ENZYME nomenclature database: | 4.3.1.23 |
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