PPO_PRUAR
ID PPO_PRUAR Reviewed; 597 AA.
AC O81103;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Polyphenol oxidase latent form, chloroplastic {ECO:0000303|PubMed:28812349};
DE Short=L-PaPPO {ECO:0000303|PubMed:28812349};
DE Short=PA-PPO {ECO:0000303|PubMed:10198084};
DE Contains:
DE RecName: Full=Polyphenol oxidase active form, chloroplastic {ECO:0000303|PubMed:28812349};
DE Short=A-PaPPO {ECO:0000303|PubMed:28812349};
DE EC=1.10.3.1 {ECO:0000269|PubMed:10198084, ECO:0000269|PubMed:28812349};
DE Flags: Precursor;
GN Name=PPO {ECO:0000303|PubMed:10198084};
OS Prunus armeniaca (Apricot) (Armeniaca vulgaris).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=36596;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 102-119, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND ACTIVITY REGULATION.
RC STRAIN=cv. Bergeron; TISSUE=Mesocarp;
RX PubMed=10198084; DOI=10.1104/pp.119.4.1261;
RA Chevalier T., de Rigal D., Mbeguie-A-Mbeguie D., Gauillard F.,
RA Richard-Forget F., Fils-Lycaon B.R.;
RT "Molecular cloning and characterization of apricot fruit polyphenol
RT oxidase.";
RL Plant Physiol. 119:1261-1270(1999).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP SPECTROMETRY, PROTEOLYTIC CLEAVAGE AT LEU-429, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=28812349; DOI=10.1021/acs.jafc.7b03210;
RA Derardja A.E., Pretzler M., Kampatsikas I., Barkat M., Rompel A.;
RT "Purification and characterization of latent polyphenol oxidase from
RT apricot (Prunus armeniaca L.).";
RL J. Agric. Food Chem. 65:8203-8212(2017).
CC -!- FUNCTION: [Polyphenol oxidase active form, chloroplastic]: Catalyzes
CC the oxidation of mono- and o-diphenols to o-diquinones. Uses
CC preferentially 4-methylcatechol and chlorogenic acid as substrates,
CC followed by caffeic acid, pyrogallol, and catechol, but barely active
CC toward dopamine and L-dopa. No activity detected with monophenols (e.g.
CC phenol and tyramine). {ECO:0000269|PubMed:28812349}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O;
CC Xref=Rhea:RHEA:21632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17253, ChEBI:CHEBI:18135; EC=1.10.3.1;
CC Evidence={ECO:0000269|PubMed:10198084, ECO:0000269|PubMed:28812349};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC -!- ACTIVITY REGULATION: Activated in the presence of substrate at low pH
CC (PubMed:28812349). Specific activity fluctuates during fruit ripening,
CC starting at immature-green stage, reaching a peak at the breaker stage,
CC followed by a sharp decrease until the half-ripe stage to remain stable
CC during the following development stages (PubMed:10198084). Triggered by
CC CuSO(4) and by low concentrations of SDS. Repressed by several
CC inhibitors including 4-hexylresorcinol, ascorbic acid, benzoic acid,
CC kojic acid, glutathione (reduced form), L-cysteine and sodium
CC metabisulfite. Inhibited by various salt such as FeSO(4), KCl, NaCl,
CC CaCl(2), MnCl(2), NiCl(2) and AlCl(3). Spontaneously activated during
CC storage at 4 degrees Celsius (PubMed:28812349).
CC {ECO:0000269|PubMed:10198084, ECO:0000269|PubMed:28812349}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 mM for 4-methylcatechol {ECO:0000269|PubMed:28812349};
CC KM=2.7 mM for chlorogenic acid {ECO:0000269|PubMed:28812349};
CC KM=5.3 mM for catechol {ECO:0000269|PubMed:28812349};
CC KM=11 mM for pyrogallol {ECO:0000269|PubMed:28812349};
CC Note=kcat is 700 sec(-1) with 4-methylcatechol as substrate. kcat is
CC 1400 sec(-1) with chlorogenic acid as substrate. kcat is 210 sec(-1)
CC with catechol as substrate. kcat is 590 sec(-1) with pyrogallol as
CC substrate. {ECO:0000269|PubMed:28812349};
CC pH dependence:
CC Optimum pH is 4.5 with catechol as substrate.
CC {ECO:0000269|PubMed:28812349};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius with catechol as substrate.
CC Completely inactivated after heating at 70 degrees Celsius for 10
CC min. {ECO:0000269|PubMed:28812349};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9ZP19}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000250|UniProtKB:Q6UIL3}.
CC -!- TISSUE SPECIFICITY: Expressed in immature-green fruit.
CC {ECO:0000269|PubMed:10198084}.
CC -!- DEVELOPMENTAL STAGE: Transcripts are highly expressed in young,
CC immature-green fruit, but turned off early in the ripening process. By
CC contrast, protein levels seem stable throughout fruit ripening.
CC {ECO:0000269|PubMed:10198084}.
CC -!- MASS SPECTROMETRY: [Polyphenol oxidase active form, chloroplastic]:
CC Mass=37455.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:28812349};
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF020786; AAC28935.1; -; mRNA.
DR AlphaFoldDB; O81103; -.
DR SMR; O81103; -.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004097; F:catechol oxidase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046148; P:pigment biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR016213; Polyphenol_oxidase.
DR InterPro; IPR022740; Polyphenol_oxidase_C.
DR InterPro; IPR022739; Polyphenol_oxidase_cen.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF12142; PPO1_DWL; 1.
DR Pfam; PF12143; PPO1_KFDV; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PIRSF; PIRSF000290; PPO_plant; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Copper; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Oxidoreductase; Plastid; Thioether bond; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000305|PubMed:10198084"
FT TRANSIT 50..101
FT /note="Thylakoid"
FT /evidence="ECO:0000305|PubMed:10198084"
FT CHAIN 102..597
FT /note="Polyphenol oxidase latent form, chloroplastic"
FT /id="PRO_0000443297"
FT CHAIN 102..429
FT /note="Polyphenol oxidase active form, chloroplastic"
FT /id="PRO_0000443298"
FT REGION 49..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 188
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 209
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 218
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 341
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 345
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 375
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT SITE 429..430
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:28812349"
FT DISULFID 112..128
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT DISULFID 127..189
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CROSSLNK 192..209
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
SQ SEQUENCE 597 AA; 67133 MW; 1B0A0FC3B1E10208 CRC64;
MATAPSPTTM GTYSSLISTN SFSTFLPNKS QLSLSGKSKH YVARRSSISC KATNNNNSNN
QNEQQEESSR LLGKLDRRNI LIGLGGLYGA TTLDRKPFAF ADPIAPPDLT TCKPAEITPG
GSETVPCCPP VTTKIKTFKP DLSIPLRTSP AAHQVTDEYL AKFKKAQAAM RALPDDDPRS
MVQQAKVHCA YCNGAYPQVG FTDNDIQVHF SWLFFPFHRM YLYFYERILG KLIDDPTFAL
PYWNWDSPVG FPIPDIYTDT SSPLYDQYRN ADHQPPVLVD LSYGGKDDDV DEQTRIDENL
AIMYRQMVSG AKTPDLFFGH AYRAGNLNTG KYPGTIENMP HNNIHIWVGD PSQTHQEDMG
NFYSAGRDPL FYAHHANVDR MWNIWKTLGG KRKDITDTDW LDAEFLFYDE NAELVRVKVR
DSLEPEKQLR YNYEPVSLPW LFTKPTARKT KNKTKAKVAA TQLTSKFPAT LVEVTTVEVA
RPKPRKRSKK EKVDEEELLI IKDIEFEGTE AVKFDVFIND DAESLSRRDK SEFAGSFVHV
PQGKTTKAKT KTNLKLGITD LLEDLGAEDD SSVLVTLVPR VSNSPITIGG FKIEYSS
