KEGG   ENZYME: 4.3.1.25Help
Entry
EC 4.3.1.25                 Enzyme                                 

Name
phenylalanine/tyrosine ammonia-lyase;
PTAL;
bifunctional PAL
Class
Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases
BRITE hierarchy
Sysname
L-phenylalanine(or L-tyrosine):trans-cinnamate(or trans-p-hydroxycinnamate) ammonia-lyase
Reaction(IUBMB)
(1) L-phenylalanine = trans-cinnamate + NH3 [RN:R00697];
(2) L-tyrosine = trans-p-hydroxycinnamate + NH3 [RN:R00737]
Reaction(KEGG)
R00697 R00737;
(other) R06132
Show
Substrate
L-phenylalanine [CPD:C00079];
L-tyrosine [CPD:C00082]
Product
trans-cinnamate [CPD:C00423];
NH3 [CPD:C00014];
trans-p-hydroxycinnamate [CPD:C00811]
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 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.24 (phenylalanine ammonia-lyase). The enzyme from some monocots, including maize, and from the yeast Rhodosporidium toruloides, deaminate L-phenylalanine and L-tyrosine with similar catalytic efficiency [3]. 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 [4].
History
EC 4.3.1.25 created 2008 (EC 4.3.1.5 created 1965, part-incorporated 2008)
Pathway
ec00360  Phenylalanine metabolism
ec00940  Phenylpropanoid biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K13064  phenylalanine/tyrosine ammonia-lyase
Genes
OSA: 4330034
DOSA: Os02t0626100-01(Os02g0626100) Os04t0518100-01(Os04g0518100)
BDI: 100839236
SBI: 8054282 8074774
ZMA: 542258(pal3)
SITA: 101756300 101780319
Taxonomy
Reference
1  [PMID:9008393]
  Authors
Rosler J, Krekel F, Amrhein N, Schmid J.
  Title
Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity.
  Journal
Plant Physiol 113:175-9 (1997)
  Sequence
[zma:542258]
Reference
2  [PMID:17185227]
  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
Chem Biol 13:1317-26 (2006)
DOI:10.1016/j.chembiol.2006.10.008
Reference
3  [PMID:17185228]
  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
Chem Biol 13:1327-38 (2006)
DOI:10.1016/j.chembiol.2006.11.011
Reference
4  [PMID:10220322]
  Authors
Schwede TF, Retey J, Schulz GE.
  Title
Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.
  Journal
Biochemistry 38:5355-61 (1999)
DOI:10.1021/bi982929q
Other DBs
ExplorEnz - The Enzyme Database: 4.3.1.25
IUBMB Enzyme Nomenclature: 4.3.1.25
ExPASy - ENZYME nomenclature database: 4.3.1.25
BRENDA, the Enzyme Database: 4.3.1.25

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