KEGG   ENZYME: 4.3.1.25
Entry
EC 4.3.1.25                 Enzyme                                 
Name
phenylalanine/tyrosine ammonia-lyase;
PTAL;
bifunctional PAL
Class
Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases
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
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
OSA4330034
DOSAOs02t0626100-01(Os02g0626100) Os04t0518100-01(Os04g0518100)
OBR102717680
BDI100839236
ATS109753501 109753502 109764465 109782978 109783107 109786255
TDC119270978 119279096 119280476 119317181 119320474
TAES123057580 123064291 123064383 123073645 123073646 123099255 123100813 123137534 123144878 542819
SBI8054282 8074774
ZMA542258
SITA101756300 101766005 101780319
SVS117861038 117862866 117864498
PVIR120656506 120709319
PHAI112882472
 » show all
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)
DOI:10.1104/pp.113.1.175
  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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