Detail Information for IndEnz0010000937
IED ID IndEnz0010000937
Enzyme Type ID esterase000937
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