KEGG   ORTHOLOGY: K10775Help
Entry
K10775                      KO                                     

Name
PAL
Definition
phenylalanine ammonia-lyase [EC:4.3.1.24]
Pathway
Phenylalanine metabolism
Phenylpropanoid biosynthesis
Module
M00039  
Monolignol biosynthesis, phenylalanine/tyrosine  => monolignol
M00137  
Flavanone biosynthesis, phenylalanine => naringenin
M00350  
Capsaicin biosynthesis, L-Phenylalanine => Capsaicin
Brite
KEGG Orthology (KO) [BR:ko00001]
 Metabolism
  Amino acid metabolism
   00360 Phenylalanine metabolism
    K10775  PAL; phenylalanine ammonia-lyase
  Biosynthesis of other secondary metabolites
   00940 Phenylpropanoid biosynthesis
    K10775  PAL; phenylalanine ammonia-lyase
KEGG modules [BR:ko00002]
 Pathway module
  Nucleotide and amino acid metabolism
   Aromatic amino acid metabolism
    M00350  Capsaicin biosynthesis, L-Phenylalanine => Capsaicin
     K10775  PAL; phenylalanine ammonia-lyase
  Secondary metabolism
   Biosynthesis of secondary metabolites
    M00039  Monolignol biosynthesis, phenylalanine / tyrosine  => monolignol
     K10775  PAL; phenylalanine ammonia-lyase
    M00137  Flavanone biosynthesis, phenylalanine => naringenin
     K10775  PAL; phenylalanine ammonia-lyase
Enzymes [BR:ko01000]
 4. Lyases
  4.3  Carbon-nitrogen lyases
   4.3.1  Ammonia-lyases
    4.3.1.24  phenylalanine ammonia-lyase
     K10775  PAL; phenylalanine ammonia-lyase
BRITE hierarchy
Other DBs
RN: 
GO: 
Genes
RSS: 
HRO: 
ATH: 
AT2G37040(PAL1) AT3G10340(PAL4) AT3G53260(PAL2) AT5G04230(PAL3)
ALY: 
CRB: 
EUS: 
BRP: 
BNA: 
THJ: 
CIT: 
CIC: 
TCC: 
GRA: 
GHI: 
EGR: 
GMX: 
PVU: 
VRA: 
VAR: 
CCAJ: 
MTR: 
CAM: 
ADU: 
AIP: 
LJA: 
Lj0g3v0106179.1(Lj0g3v0106179.1) Lj0g3v0106189.1(Lj0g3v0106189.1) Lj0g3v0121549.1(Lj0g3v0121549.1) Lj0g3v0245929.1(Lj0g3v0245929.1) Lj0g3v0269169.1(Lj0g3v0269169.1) Lj0g3v0269199.1(Lj0g3v0269199.1) Lj0g3v0269209.1(Lj0g3v0269209.1) Lj0g3v0350889.1(Lj0g3v0350889.1) Lj1g3v4590760.1(Lj1g3v4590760.1) Lj1g3v4590760.2(Lj1g3v4590760.2) Lj1g3v4590760.3(Lj1g3v4590760.3) Lj1g3v4590770.1(Lj1g3v4590770.1) Lj1g3v4590840.1(Lj1g3v4590840.1) Lj1g3v4590850.1(Lj1g3v4590850.1) Lj1g3v4590850.2(Lj1g3v4590850.2) Lj2g3v3339740.1(Lj2g3v3339740.1) Lj3g3v0602620.1(Lj3g3v0602620.1) Lj3g3v0602630.1(Lj3g3v0602630.1) Lj3g3v0602630.2(Lj3g3v0602630.2) Lj3g3v0602650.1(Lj3g3v0602650.1) Lj5g3v0659760.1(Lj5g3v0659760.1) Lj5g3v1811400.1(Lj5g3v1811400.1)
LANG: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
ZJU: 
CSV: 
CMO: 
RCU: 
JCU: 
POP: 
POPTR_0006s12870g POPTR_0008s03810g(POPTRDRAFT_820249) POPTR_0010s23100g(POPTRDRAFT_822571) POPTR_0010s23110g(POPTRDRAFT_228016) POPTR_0016s09230g(POPTRDRAFT_667815)
VVI: 
SLY: 
SPEN: 
SOT: 
INI: 
SIND: 
BVG: 
NNU: 
OSA: 
4330036(P0042D01.4) 4330037(P0042D01.5) 4330040(OsJ_007359) 4336415 4338861
DOSA: 
Os02t0626400-01(Os02g0626400) Os02t0626600-00(Os02g0626600) Os02t0627100-01(Os02g0627100) Os04t0518400-01(Os04g0518400) Os05t0427400-00(Os05g0427400) Os12t0520200-01(Os12g0520200)
OBR: 
BDI: 
ATS: 
SBI: 
ZMA: 
SITA: 
PDA: 
EGU: 
MUS: 
ATR: 
SMO: 
PPP: 
NCR: 
NTE: 
NEUTE1DRAFT85424(NEUTE1DRAFT_85424)
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
FGR: 
FPU: 
FVR: 
FOX: 
NHE: 
MAW: 
MAJ: 
VAL: 
VDA: 
CFJ: 
ELA: 
PFY: 
BFU: 
PSCO: 
ANI: 
AFM: 
AOR: 
AOR_1_1090114(AO090701000601) AOR_1_1318054(AO090011000788) AOR_1_1676014(AO090026000586) AOR_1_934174(AO090005000532)
ANG: 
ANI_1_1828184(An04g04370) ANI_1_2142074(An08g07740) ANI_1_738114(An13g02640)
AFV: 
ACT: 
NFI: 
PCS: 
URE: 
PNO: 
PTE: 
BZE: 
BCOM: 
NPA: 
TVS: 
DSQ: 
PCO: 
SHS: 
HIR: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT112726(AGABI1DRAFT_112726) AGABI1DRAFT112810(AGABI1DRAFT_112810)
ABV: 
CPUT: 
SLA: 
UMA: 
PFP: 
PGR: 
MLR: 
YEN: 
YEP: 
YEY: 
YEW: 
YET: 
YEF: 
YEE: 
PLU: 
PAY: 
PTT: 
NCO: 
RXY: 
GLP: 
NPU: 
AVA: 
RIV: 
SCS: 
PBS: 
AG: 
CAA57056(PAL2) CAA57057(PAL3) CAA68938(PAL1)
 » show all
TaxonomyKoalaUniProt
LinkDB All DBs

KEGG   ORTHOLOGY: K13064Help
Entry
K13064                      KO                                     

Name
PTAL
Definition
phenylalanine/tyrosine ammonia-lyase [EC:4.3.1.25]
Pathway
Phenylalanine metabolism
Phenylpropanoid biosynthesis
Module
M00039  
Monolignol biosynthesis, phenylalanine/tyrosine  => monolignol
M00350  
Capsaicin biosynthesis, L-Phenylalanine => Capsaicin
Brite
KEGG Orthology (KO) [BR:ko00001]
 Metabolism
  Amino acid metabolism
   00360 Phenylalanine metabolism
    K13064  PTAL; phenylalanine/tyrosine ammonia-lyase
  Biosynthesis of other secondary metabolites
   00940 Phenylpropanoid biosynthesis
    K13064  PTAL; phenylalanine/tyrosine ammonia-lyase
KEGG modules [BR:ko00002]
 Pathway module
  Nucleotide and amino acid metabolism
   Aromatic amino acid metabolism
    M00350  Capsaicin biosynthesis, L-Phenylalanine => Capsaicin
     K13064  PTAL; phenylalanine/tyrosine ammonia-lyase
  Secondary metabolism
   Biosynthesis of secondary metabolites
    M00039  Monolignol biosynthesis, phenylalanine / tyrosine  => monolignol
     K13064  PTAL; phenylalanine/tyrosine ammonia-lyase
Enzymes [BR:ko01000]
 4. Lyases
  4.3  Carbon-nitrogen lyases
   4.3.1  Ammonia-lyases
    4.3.1.25  phenylalanine/tyrosine ammonia-lyase
     K13064  PTAL; phenylalanine/tyrosine ammonia-lyase
BRITE hierarchy
Other DBs
Genes
OSA: 
4330034(P0042D01.1)
DOSA: 
Os02t0626100-01(Os02g0626100) Os04t0518100-01(Os04g0518100)
BDI: 
SBI: 
ZMA: 
542258(pal3)
SITA: 
TaxonomyKoalaUniProt
Reference
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]
LinkDB All DBs

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
RSS: 
HRO: 
ATH: 
AT2G37040(PAL1) AT3G10340(PAL4) AT3G53260(PAL2) AT5G04230(PAL3)
ALY: 
CRB: 
EUS: 
BRP: 
BNA: 
THJ: 
CIT: 
CIC: 
TCC: 
GRA: 
GHI: 
EGR: 
GMX: 
PVU: 
VRA: 
VAR: 
CCAJ: 
MTR: 
CAM: 
ADU: 
AIP: 
LJA: 
Lj0g3v0106179.1(Lj0g3v0106179.1) Lj0g3v0106189.1(Lj0g3v0106189.1) Lj0g3v0121549.1(Lj0g3v0121549.1) Lj0g3v0245929.1(Lj0g3v0245929.1) Lj0g3v0269169.1(Lj0g3v0269169.1) Lj0g3v0269199.1(Lj0g3v0269199.1) Lj0g3v0269209.1(Lj0g3v0269209.1) Lj0g3v0350889.1(Lj0g3v0350889.1) Lj1g3v4590760.1(Lj1g3v4590760.1) Lj1g3v4590760.2(Lj1g3v4590760.2) Lj1g3v4590760.3(Lj1g3v4590760.3) Lj1g3v4590770.1(Lj1g3v4590770.1) Lj1g3v4590840.1(Lj1g3v4590840.1) Lj1g3v4590850.1(Lj1g3v4590850.1) Lj1g3v4590850.2(Lj1g3v4590850.2) Lj2g3v3339740.1(Lj2g3v3339740.1) Lj3g3v0602620.1(Lj3g3v0602620.1) Lj3g3v0602630.1(Lj3g3v0602630.1) Lj3g3v0602630.2(Lj3g3v0602630.2) Lj3g3v0602650.1(Lj3g3v0602650.1) Lj5g3v0659760.1(Lj5g3v0659760.1) Lj5g3v1811400.1(Lj5g3v1811400.1)
LANG: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
ZJU: 
CSV: 
CMO: 
RCU: 
JCU: 
POP: 
POPTR_0006s12870g POPTR_0008s03810g(POPTRDRAFT_820249) POPTR_0010s23100g(POPTRDRAFT_822571) POPTR_0010s23110g(POPTRDRAFT_228016) POPTR_0016s09230g(POPTRDRAFT_667815)
VVI: 
SLY: 
SPEN: 
SOT: 
INI: 
SIND: 
BVG: 
NNU: 
OSA: 
4330036(P0042D01.4) 4330037(P0042D01.5) 4330040(OsJ_007359) 4336415 4338861
DOSA: 
Os02t0626400-01(Os02g0626400) Os02t0626600-00(Os02g0626600) Os02t0627100-01(Os02g0627100) Os04t0518400-01(Os04g0518400) Os05t0427400-00(Os05g0427400) Os12t0520200-01(Os12g0520200)
OBR: 
BDI: 
ATS: 
SBI: 
ZMA: 
SITA: 
PDA: 
EGU: 
MUS: 
ATR: 
SMO: 
PPP: 
NCR: 
NTE: 
NEUTE1DRAFT85424(NEUTE1DRAFT_85424)
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
FGR: 
FPU: 
FVR: 
FOX: 
NHE: 
MAW: 
MAJ: 
VAL: 
VDA: 
CFJ: 
ELA: 
PFY: 
BFU: 
PSCO: 
ANI: 
AFM: 
AOR: 
AOR_1_1090114(AO090701000601) AOR_1_1318054(AO090011000788) AOR_1_1676014(AO090026000586) AOR_1_934174(AO090005000532)
ANG: 
ANI_1_1828184(An04g04370) ANI_1_2142074(An08g07740) ANI_1_738114(An13g02640)
AFV: 
ACT: 
NFI: 
PCS: 
URE: 
PNO: 
PTE: 
BZE: 
BCOM: 
NPA: 
TVS: 
DSQ: 
PCO: 
SHS: 
HIR: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT112726(AGABI1DRAFT_112726) AGABI1DRAFT112810(AGABI1DRAFT_112810)
ABV: 
CPUT: 
SLA: 
UMA: 
PFP: 
PGR: 
MLR: 
YEN: 
YEP: 
YEY: 
YEW: 
YET: 
YEF: 
YEE: 
PLU: 
PAY: 
PTT: 
NCO: 
RXY: 
GLP: 
NPU: 
AVA: 
RIV: 
SCS: 
PBS: 
 » 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
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
LinkDB All DBs

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
Phenylalanine metabolism
Phenylpropanoid biosynthesis
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K13064  
phenylalanine/tyrosine ammonia-lyase
Genes
OSA: 
4330034(P0042D01.1)
DOSA: 
Os02t0626100-01(Os02g0626100) Os04t0518100-01(Os04g0518100)
BDI: 
SBI: 
ZMA: 
542258(pal3)
SITA: 
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 (1997) 175-9.
  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 (2006) 1317-26.
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: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: 
LinkDB All DBs

KEGG   REACTION: R00697Help
Entry
R00697                      Reaction                               

Name
L-phenylalanine ammonia-lyase (trans-cinnamate-forming)
Definition
L-Phenylalanine <=> trans-Cinnamate + Ammonia
Equation
Reaction class
C00079_C00423
Enzyme
4.3.1.24        4.3.1.25
Pathway
Phenylalanine metabolism
Phenylpropanoid biosynthesis
Metabolic pathways
Biosynthesis of secondary metabolites
Module
M00039  
Monolignol biosynthesis, phenylalanine/tyrosine  => monolignol
M00137  
Flavanone biosynthesis, phenylalanine => naringenin
M00350  
Capsaicin biosynthesis, L-Phenylalanine => Capsaicin
Orthology
K10775  
phenylalanine ammonia-lyase [EC:4.3.1.24]
K13064  
phenylalanine/tyrosine ammonia-lyase [EC:4.3.1.25]
LinkDB All DBs

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