IED ID | IndEnz0005001300 |
Enzyme Type ID | lipase001300 |
Protein Name |
GDSL esterase/lipase At3g26430 EC 3.1.1.- Extracellular lipase At3g26430 |
Gene Name | At3g26430 F20C19.19 |
Organism | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
Enzyme Sequence | METNLLLVKCVLLASCLIHPRACSPSCNFPAIFNFGDSNSDTGGLSASFGQAPYPNGQTFFHSPSGRFSDGRLIIDFIAEELGLPYLNAFLDSIGSNFSHGANFATAGSTVRPPNATIAQSGVSPISLDVQLVQFSDFITRSQLIRNRGGVFKKLLPKKEYFSQALYTFDIGQNDLTAGLKLNMTSDQIKAYIPDVHDQLSNVIRKVYSKGGRRFWIHNTAPLGCLPYVLDRFPVPASQIDNHGCAIPRNEIARYYNSELKRRVIELRKELSEAAFTYVDIYSIKLTLITQAKKLGFRYPLVACCGHGGKYNFNKLIKCGAKVMIKGKEIVLAKSCNDVSFRVSWDGIHFTETTNSWIFQQINDGAFSDPPLPVKSACTR |
Enzyme Length | 380 |
Uniprot Accession Number | Q9LIN2 |
Absorption | |
Active Site | ACT_SITE 38; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P0ADA1; ACT_SITE 346; /evidence=ECO:0000250|UniProtKB:P0ADA1; ACT_SITE 349; /evidence=ECO:0000250|UniProtKB:P0ADA1 |
Activity Regulation | ACTIVITY REGULATION: Lipase activity is inhibited by phenylmethylsulfonyl fluoride (PMSF), but not neostigmine bromide (NB). {ECO:0000269|PubMed:23430565}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) + hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:23430565};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393; Evidence={ECO:0000269|PubMed:23430565}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:23430565};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:23430565}; |
DNA Binding | |
EC Number | 3.1.1.- |
Enzyme Function | FUNCTION: Lipase that can hydrolyze p-nitrophenyl butyrate and p-nitrophenyl palmitate in vitro (PubMed:23430565). Possesses low activity against p-nitrophenyl acetate (PubMed:23430565). Substrate preference is p-nitrophenyl palmitate > p-nitrophenyl butyrate >> p-nitrophenyl acetate (PubMed:23430565). Lacks cholinesterase activity (PubMed:23430565). {ECO:0000269|PubMed:23430565}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Glycosylation (3); Signal peptide (1) |
Keywords | Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 15659355; 28840447; |
Motif | |
Gene Encoded By | |
Mass | 42,062 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:23430565}; KM=2.0 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:23430565}; KM=1.2 mM for p-nitrophenyl palmitate {ECO:0000269|PubMed:23430565}; |
Metal Binding | |
Rhea ID | RHEA:47392; RHEA:47393; RHEA:47348; RHEA:47349 |
Cross Reference Brenda |