HPAAS_PETCR
ID HPAAS_PETCR Reviewed; 514 AA.
AC Q06086; A0A140F7X7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=4-hydroxyphenylacetaldehyde synthase {ECO:0000303|PubMed:22266321};
DE Short=HPAA synthase {ECO:0000305};
DE EC=4.1.1.108 {ECO:0000269|PubMed:22266321, ECO:0000269|PubMed:23204519, ECO:0000269|PubMed:31682615};
DE AltName: Full=3,4-dihydroxyphenylacetaldehyde synthase {ECO:0000305};
DE Short=DHPAA synthase {ECO:0000305};
DE EC=4.1.1.107 {ECO:0000269|PubMed:22266321, ECO:0000269|PubMed:31682615};
DE AltName: Full=Aromatic acetaldehyde synthase {ECO:0000303|PubMed:31682615};
DE Short=PcAAS {ECO:0000303|PubMed:31682615};
GN Name=AAS {ECO:0000303|PubMed:31682615};
GN Synonyms=TDC {ECO:0000303|PubMed:22266321},
GN TYRDC-2 {ECO:0000303|PubMed:8420986};
OS Petroselinum crispum (Parsley) (Petroselinum hortense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Petroselinum.
OX NCBI_TaxID=4043;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY FUNGAL ELICITOR.
RX PubMed=8420986; DOI=10.1016/s0021-9258(18)53980-6;
RA Kawalleck P., Keller H., Hahlbrock K., Scheel D., Somssich I.E.;
RT "A pathogen-responsive gene of parsley encodes tyrosine decarboxylase.";
RL J. Biol. Chem. 268:2189-2194(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOTECHNOLOGY.
RX PubMed=31682615; DOI=10.1371/journal.pone.0212243;
RA Trantas E., Navakoudis E., Pavlidis T., Nikou T., Halabalaki M.,
RA Skaltsounis L., Ververidis F.;
RT "Dual pathway for metabolic engineering of Escherichia coli to produce the
RT highly valuable hydroxytyrosol.";
RL PLoS ONE 14:e0212243-e0212243(2019).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP INDUCTION BY METHYL JASMONATE.
RX PubMed=22266321; DOI=10.1016/j.bbrc.2011.12.124;
RA Torrens-Spence M.P., Gillaspy G., Zhao B., Harich K., White R.H., Li J.;
RT "Biochemical evaluation of a parsley tyrosine decarboxylase results in a
RT novel 4-hydroxyphenylacetaldehyde synthase enzyme.";
RL Biochem. Biophys. Res. Commun. 418:211-216(2012).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-346.
RX PubMed=23204519; DOI=10.1074/jbc.m112.401752;
RA Torrens-Spence M.P., Liu P., Ding H., Harich K., Gillaspy G., Li J.;
RT "Biochemical evaluation of the decarboxylation and decarboxylation-
RT deamination activities of plant aromatic amino acid decarboxylases.";
RL J. Biol. Chem. 288:2376-2387(2013).
CC -!- FUNCTION: Catalyzes the production of 4-hydroxyphenylacetaldehyde
CC (HPAA) directly from L-tyrosine, tyramine not being formed as an
CC intermediate (PubMed:22266321, PubMed:23204519, PubMed:31682615).
CC Catalyzes both the decarboxylation and deamination of L-dopa to 3,4-
CC dihydroxylphenylacetaldehyde (DHPAA) (PubMed:31682615,
CC PubMed:22266321). {ECO:0000269|PubMed:22266321,
CC ECO:0000269|PubMed:23204519, ECO:0000269|PubMed:31682615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + L-tyrosine + O2 = (4-hydroxyphenyl)acetaldehyde +
CC CO2 + H2O2 + NH4(+); Xref=Rhea:RHEA:55528, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15621,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58315; EC=4.1.1.108;
CC Evidence={ECO:0000269|PubMed:22266321, ECO:0000269|PubMed:23204519,
CC ECO:0000269|PubMed:31682615};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55529;
CC Evidence={ECO:0000269|PubMed:22266321, ECO:0000269|PubMed:23204519,
CC ECO:0000269|PubMed:31682615};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + L-dopa + O2 = 3,4-dihydroxyphenylacetaldehyde +
CC CO2 + H2O2 + NH4(+); Xref=Rhea:RHEA:55524, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:27978, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57504; EC=4.1.1.107;
CC Evidence={ECO:0000269|PubMed:22266321, ECO:0000269|PubMed:31682615};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55525;
CC Evidence={ECO:0000269|PubMed:22266321, ECO:0000269|PubMed:31682615};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:22266321};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.46 mM for L-tyrosine {ECO:0000269|PubMed:22266321};
CC KM=1.4 mM for L-dopa {ECO:0000269|PubMed:22266321};
CC Vmax=1.117 umol/min/mg enzyme with L-tyrosine as substrate
CC {ECO:0000269|PubMed:22266321};
CC Vmax=0.318 umol/min/mg enzyme with L-dopa as substrate
CC {ECO:0000269|PubMed:22266321};
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- INDUCTION: Induced by fungal elicitor (PubMed:8420986). Induced by
CC methyl jasmonate (PubMed:22266321). {ECO:0000269|PubMed:22266321,
CC ECO:0000269|PubMed:8420986}.
CC -!- BIOTECHNOLOGY: TYDC-2 from parsley can be used in E.coli to produce
CC 3,4-dihydroxyphenylacetaldehyde, a direct precursor of hydroxytyrosol,
CC which is a natural compound from olive oil with a strong antioxidant
CC activity. {ECO:0000305|PubMed:31682615}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; M96070; AAA33860.1; -; mRNA.
DR EMBL; KT334544; AML79732.1; -; mRNA.
DR PIR; A44405; A44405.
DR AlphaFoldDB; Q06086; -.
DR SMR; Q06086; -.
DR KEGG; ag:AAA33860; -.
DR BRENDA; 4.1.1.108; 4694.
DR BRENDA; 4.1.1.25; 4694.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Lyase; Pyridoxal phosphate.
FT CHAIN 1..514
FT /note="4-hydroxyphenylacetaldehyde synthase"
FT /id="PRO_0000146996"
FT BINDING 100
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT BINDING 201
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT BINDING 316
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT BINDING 346
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q8RY79"
FT MOD_RES 317
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305|PubMed:22266321"
FT MUTAGEN 346
FT /note="F->Y: Abolishes 4-hydroxyphenylacetaldehyde synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:23204519"
SQ SEQUENCE 514 AA; 57450 MW; B742FB7CABB4CF39 CRC64;
MGSIDNLTEK LASQFPMNTL EPEEFRRQGH MMIDFLADYY RKVENYPVRS QVSPGYLREI
LPESAPYNPE SLETILQDVQ TKIIPGITHW QSPNFFAYFP SSGSTAGFLG EMLSTGFNVV
GFNWMVSPAA TELENVVTDW FGKMLQLPKS FLFSGGGGGV LQGTTCEAIL CTLVAARDKN
LRQHGMDNIG KLVVYCSDQT HSALQKAAKI AGIDPKNFRA IETTKSSNFQ LCPKRLESAI
LHDLQNGLIP LYLCATVGTT SSTTVDPLPA LTEVAKKYDL WVHVDAAYAG SACICPEFRQ
YLDGVENADS FSLNAHKWFL TTLDCCCLWV RNPSALIKSL STYPEFLKNN ASETNKVVDY
KDWQIMLSRR FRALKLWFVL RSYGVGQLRE FIRGHVGMAK YFEGLVNMDK RFEVVAPRLF
SMVCFRIKPS AMIGKNDEDE VNEINRKLLE SVNDSGRIYV SHTVLGGIYV IRFAIGGTLT
DINHVSAAWK VLQDHAGALL DDTFTSNKLV EVLS
