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Information on EC 4.3.1.24 - phenylalanine ammonia-lyase and Organism(s) Rhodosporidium toruloides and UniProt Accession P11544

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.24 phenylalanine ammonia-lyase
IUBMB Comments
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 . This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine . The enzyme from some species is highly specific for phenylalanine [7,8].
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This record set is specific for:
Rhodosporidium toruloides
UNIPROT: P11544
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phenylalanine ammonia-lyase, phenylalanine ammonia lyase, l-phenylalanine ammonia-lyase, dcpal1, rgpal, phe ammonia-lyase, avpal, palrs1, atpal2, sspal1, more
SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine ammonia-lyase (trans-cinnamate-forming)
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9024-28-6
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PALY_RHOTO
716
0
76880
Swiss-Prot
-