KEGG   ENZYME: 4.3.1.24Help
Entry
EC 4.3.1.24                 Enzyme                                 

Name
phenylalanine ammonia-lyase;
phenylalanine deaminase;
phenylalanine ammonium-lyase;
PAL;
L-phenylalanine ammonia-lyase;
Phe ammonia-lyase
Class
Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases
BRITE hierarchy
Sysname
L-phenylalanine ammonia-lyase (trans-cinnamate-forming)
Reaction(IUBMB)
L-phenylalanine = trans-cinnamate + NH3 [RN:R00697]
Reaction(KEGG)
R00697;
(other) R06132
Show
Substrate
L-phenylalanine [CPD:C00079]
Product
trans-cinnamate [CPD:C00423];
NH3 [CPD:C00014]
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].
History
EC 4.3.1.24 created 2008 (EC 4.3.1.5 created 1965, part-incorporated 2008)
Pathway
Phenylalanine metabolism
Phenylpropanoid biosynthesis
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K10775  
phenylalanine ammonia-lyase
Genes
ATH: 
AT2G37040(PAL1) AT3G10340(PAL4) AT3G53260(PAL2) AT5G04230(PAL3)
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
PMUM: 
MDM: 
CSV: 
CMO: 
RCU: 
POP: 
POPTR_0006s12870g POPTR_0008s03810g(POPTRDRAFT_820249) POPTR_0010s23100g(POPTRDRAFT_822571) POPTR_0010s23110g(POPTRDRAFT_228016) POPTR_0016s09230g(POPTRDRAFT_667815)
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os02t0626400-01(Os02g0626400) Os02t0626600-00(Os02g0626600) Os02t0627100-01(Os02g0627100) Os04t0518400-01(Os04g0518400) Os05t0427400-00(Os05g0427400) Os12t0520200-01(Os12g0520200)
OBR: 
BDI: 
SBI: 
SORBI_01g014020(SORBIDRAFT_01g014020) SORBI_04g026520(SORBIDRAFT_04g026520) SORBI_04g026530(SORBIDRAFT_04g026530) SORBI_04g026540(SORBIDRAFT_04g026540) SORBI_04g026550(SORBIDRAFT_04g026550) SORBI_04g026560(SORBIDRAFT_04g026560) SORBI_06g022750(SORBIDRAFT_06g022750)
ZMA: 
SITA: 
ATR: 
s00024p00201680(AMTR_s00024p00201680) s00024p00201930(AMTR_s00024p00201930) s00024p00202590(AMTR_s00024p00202590) s00032p00159210(AMTR_s00032p00159210) s00148p00088930(AMTR_s00148p00088930)
SMO: 
PPP: 
YEN: 
PLU: 
PAY: 
RXY: 
PBS: 
GLP: 
NPU: 
AVA: 
RIV: 
SCS: 
 » show all
Taxonomy
Reference
1  [PMID:14458851]
  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 (1961) 2692-8.
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 (1966) 1121-1132.
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 (2006) 1327-38.
Reference
4  [PMID:15350127]
  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
Biochemistry. 43 (2004) 11403-16.
Reference
5  [PMID:15548745]
  Authors
Ritter H, Schulz GE.
  Title
Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase.
  Journal
Plant. Cell. 16 (2004) 3426-36.
  Sequence
[up:P24481]
Reference
6  [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 (2006) 1317-26.
  Sequence
Reference
7  [PMID:7925471]
  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
Eur. J. Biochem. 225 (1994) 491-9.
  Sequence
Reference
8  [PMID:15276452]
  Authors
Cochrane FC, Davin LB, Lewis NG.
  Title
The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.
  Journal
Phytochemistry. 65 (2004) 1557-64.
  Sequence
Reference
9  [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 (1999) 5355-61.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9024-28-6

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