| IED ID | IndEnz0005000522 |
| Enzyme Type ID | lipase000522 |
| Protein Name |
Patatin-B2 EC 3.1.1.- |
| Gene Name | PATB2 |
| Organism | Solanum tuberosum (Potato) |
| 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 tuberosum (Potato) |
| Enzyme Sequence | MATTKSFLILFFMILATTSSTCAKLEEMVTVLSIDGGGIKGIIPAIILEFLEGQLQEVDNNKDARLADYFDVIGGTSTGGLLTAMITTPNENNRPFAAAKDIVPFYFEHGPHIFNYSGSILGPMYDGKYLLQVLQEKLGETRVHQALTEVAISSFDIKTNKPVIFTKSNLAKSPELDAKMYDICYSTAAAPIYFPPHHFVTHTSNGARYEFNLVDGAVATVGDPALLSLSVATRLAQEDPAFSSIKSLDYKQMLLLSLGTGTNSEFDKTYTAEEAAKWGPLRWMLAIQQMTNAASSYMTDYYISTVFQARHSQNNYLRVQENALNGTTTEMDDASEANMELLVQVGETLLKKPVSKDSPETYEEALKRFAKLLSDRKKLRANKASH |
| Enzyme Length | 386 |
| Uniprot Accession Number | P15477 |
| Absorption | |
| Active Site | ACT_SITE 77; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 215; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by methyl-p-nitrophenyl-octylphosphonate. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Lipolytic acyl hydrolase (LAH), an activity which is thought to be involved in the response of tubers to pathogens. Can use p-nitrophenyl esters as substrates with highest activity on p-nitrophenyl caprate (C10). Also active on mono-acylglycolphosphocholines and diacylphospholipids, with highest specific activities observed were obtained with the synthetic phospholipids diC8PCho and diC9PCho. Mono-olein and myverol can also be hydrolyzed. {ECO:0000269|PubMed:11589694}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Glycosylation (2); Motif (3); Mutagenesis (6); Signal peptide (1) |
| Keywords | Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Plant defense;Reference proteome;Signal;Storage protein;Vacuole |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 36..41; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 75..79; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 215..217; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 42,613 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=At pH 8.0, the highest specific activity is observed with phospholipids such as diC8PCho and diC9PCho and with p-nitrophenyl esters such as p-nitrophenyl caprate. {ECO:0000269|PubMed:11589694}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |