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
ec00360  Phenylalanine metabolism
ec00940  Phenylpropanoid biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K10775  phenylalanine ammonia-lyase
Genes
RSS: 109440234 109440235
HRO: HELRODRAFT_78004 HELRODRAFT_78007
LAK: 106161379 106161381 106161385 106172274 106172288
ATH: AT2G37040(PAL1) AT3G10340(PAL4) AT3G53260(PAL2) AT5G04230(PAL3)
ALY: ARALYDRAFT_482690 ARALYDRAFT_487203(PAL3) ARALYDRAFT_655277 ARALYDRAFT_897210 ARALYDRAFT_906713(PAL2)
CRB: 17885805 17889220 17892444
CSAT: 104704772 104711886 104745212 104761517 104781181 104782125 104785814 104789427 104791591 104792487 109131978
EUS: EUTSA_v10010153mg EUTSA_v10016314mg EUTSA_v10020168mg
BRP: 103829920 103841251 103849325 103864245 103865574(PAL-BR-1) 103867229(PAL) 103870475
BNA: 106352757 106355487 106371447 106371449 106371451 106377171 106382579 106384062 106388513 106388514 106388515 106389127 106391500 106398793 106452446 106452673 111197696 111207414 111211703
GMX: 100302735(GMPAL2.1) 100787872(GMPAL3.1) 100787902(GMPAL1.3) 100788438(GMPAL1.2) 100801470(GMPAL2.4) 100803857(GMPAL2.3) 100811101(GMPAL1.1) 100818777(GMPAL2.2)
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)
BVG: 104898673
SOE: 110796050
DOSA: Os02t0626400-01(Os02g0626400) Os02t0626600-00(Os02g0626600) Os02t0627100-01(Os02g0627100) Os04t0518400-01(Os04g0518400) Os05t0427400-00(Os05g0427400) Os12t0520200-01(Os12g0520200)
ATS: 109736056(LOC109736056) 109750201(LOC109750201) 109750202(LOC109750202) 109750206(LOC109750206) 109750207(LOC109750207) 109752036(LOC109752036) 109752043(LOC109752043) 109758771(LOC109758771) 109758772(LOC109758772) 109758784(LOC109758784) 109758790(LOC109758790) 109760444(LOC109760444) 109764463(LOC109764463) 109764464(LOC109764464) 109767405(LOC109767405) 109777317(LOC109777317)
NCR: NCU09391
NTE: NEUTE1DRAFT85424(NEUTE1DRAFT_85424)
MGR: MGG_10036
SSCK: SPSK_07118
MAW: MAC_06002
ANI: AN6075.2
ANG: ANI_1_1828184(An04g04370) ANI_1_2142074(An08g07740) ANI_1_738114(An13g02640)
PTE: PTT_11854
ABP: AGABI1DRAFT112726(AGABI1DRAFT_112726) AGABI1DRAFT112810(AGABI1DRAFT_112810)
YEN: YE3021
YEY: Y11_19441
YEW: CH47_2390
YET: CH48_2792
PLU: plu2234
PAY: PAU_02187
RXY: Rxyl_1739
AVA: Ava_3988
 » 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 236:2692-8 (1961)
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 5:1121-1132 (1966)
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: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 43:11403-16 (2004)
DOI:10.1021/bi049053+
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 16:3426-36 (2004)
DOI:10.1105/tpc.104.025288
  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 13:1317-26 (2006)
DOI:10.1016/j.chembiol.2006.10.008
  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 225:491-9 (1994)
DOI:10.1111/j.1432-1033.1994.00491.x
  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 65:1557-64 (2004)
DOI:10.1016/j.phytochem.2004.05.006
  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 38:5355-61 (1999)
DOI:10.1021/bi982929q
Other DBs
ExplorEnz - The Enzyme Database: 4.3.1.24
IUBMB Enzyme Nomenclature: 4.3.1.24
ExPASy - ENZYME nomenclature database: 4.3.1.24
BRENDA, the Enzyme Database: 4.3.1.24
CAS: 9024-28-6

DBGET integrated database retrieval system