Detail Information for IndEnz0003000003
IED ID IndEnz0003000003
Enzyme Type ID pectinase000003
Protein Name Polygalacturonase-2
PG
EC 3.2.1.15
PG-2A
PG-2B
Pectinase
Gene Name PG2 PG PG2A PG2B
Organism Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Solanaceae Solanoideae Solaneae Solanum Solanum subgen. Lycopersicon Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Enzyme Sequence MVIQRNSILLLIIIFASSISTCRSNVIDDNLFKQVYDNILEQEFAHDFQAYLSYLSKNIESNNNIDKVDKNGIKVINVLSFGAKGDGKTYDNIAFEQAWNEACSSRTPVQFVVPKNKNYLLKQITFSGPCRSSISVKIFGSLEASSKISDYKDRRLWIAFDSVQNLVVGGGGTINGNGQVWWPSSCKINKSLPCRDAPTALTFWNCKNLKVNNLKSKNAQQIHIKFESCTNVVASNLMINASAKSPNTDGVHVSNTQYIQISDTIIGTGDDCISIVSGSQNVQATNITCGPGHGISIGSLGSGNSEAYVSNVTVNEAKIIGAENGVRIKTWQGGSGQASNIKFLNVEMQDVKYPIIIDQNYCDRVEPCIQQFSAVQVKNVVYENIKGTSATKVAIKFDCSTNFPCEGIIMENINLVGESGKPSEATCKNVHFNNAEHVTPHCTSLEISEDEALLYNY
Enzyme Length 457
Uniprot Accession Number P05117
Absorption BIOPHYSICOCHEMICAL PROPERTIES: Absorption: Abs(max)=276 nm {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759}; Note=The ratio of Abs(276)/Abs(260)=1.35. These values are for PG1.;
Active Site ACT_SITE 270; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10052; ACT_SITE 293; /evidence=ECO:0000255|PROSITE-ProRule:PRU10052
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=(1,4-alpha-D-galacturonosyl)(n+m) + H(2)O = (1,4-alpha-D-galacturonosyl)(n) + (1,4-alpha-D-galacturonosyl)(m).; EC=3.2.1.15; Evidence={ECO:0000269|PubMed:9701584};
DNA Binding
EC Number 3.2.1.15
Enzyme Function FUNCTION: Catalytic subunit of the polygalacturonase isozyme 1 and 2 (PG1 and PG2). Acts in concert with the pectinesterase, in the ripening process. Is involved in cell wall metabolism, specifically in polyuronide degradation. The depolymerization and solubilization of cell wall polyuronides mediated by PG2 during ripening seems to be limited by the beta subunit GP1, probably by recruiting PG2 to form PG1. {ECO:0000269|PubMed:2152163, ECO:0000269|PubMed:7827495, ECO:0000269|PubMed:9747798}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55-60 degrees Celsius at pH 4.4. PG1 is more thermostable than PG2. {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.4-4.8 at 35 degrees Celsius. PG1 is resistant to acidic but not to alkaline conditions, at which PG2 is released from the beta subunit. {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759};
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Frameshift (1); Glycosylation (4); Propeptide (2); Repeat (4); Sequence conflict (3); Signal peptide (1)
Keywords Apoplast;Cell wall;Cell wall biogenesis/degradation;Direct protein sequencing;Fruit ripening;Genetically modified food;Glycoprotein;Glycosidase;Hydrolase;Reference proteome;Repeat;Secreted;Signal
Interact With
Induction INDUCTION: By ethylene. {ECO:0000269|PubMed:12232274}.
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:2152163}. Secreted, cell wall {ECO:0000269|PubMed:2152163}. Note=Associated to the cell wall.
Modified Residue
Post Translational Modification PTM: N-glycosylated. PG2B isozyme has a greater degree of glycosylation than PG2A. {ECO:0000269|PubMed:16666031, ECO:0000269|PubMed:2152163, ECO:0000269|PubMed:6617647}.
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000269|PubMed:16666031
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 14640598; 14640599; 15113178; 15129437; 17244632; 25980771;
Motif
Gene Encoded By
Mass 50,052
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=38 uM for polygalacturonic acid (for PG2 at pH 4.6 and 35 degrees Celsius) {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759}; KM=75 uM for polygalacturonic acid (for PG1 at pH 4.6 and 35 degrees Celsius) {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759}; Vmax=58.8 umol/min/mg enzyme (for PG2 at pH 4.6 and 35 degrees Celsius) {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759}; Vmax=7 umol/min/mg enzyme (for PG2 at pH 3.8 and 25 degrees Celsius) {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759}; Vmax=27.7 umol/min/mg enzyme (for PG1 at pH 4.6 and 35 degrees Celsius) {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759}; Vmax=4 umol/min/mg enzyme (for PG1 at pH 3.8 and 25 degrees Celsius) {ECO:0000269|PubMed:15007842, ECO:0000269|PubMed:6489331, ECO:0000269|PubMed:6617647, ECO:0000269|PubMed:7449759};
Metal Binding
Rhea ID
Cross Reference Brenda