Detail Information for IndEnz0010001279
IED ID IndEnz0010001279
Enzyme Type ID esterase001279
Protein Name GDSL lipase
TcGLIP
EC 3.1.1.-
Pyrethrin type I synthase
Gene Name GLIP
Organism Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum cinerariifolium)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids campanulids Asterales Asteraceae Asteroideae Anthemideae Anthemidinae Tanacetum Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum cinerariifolium)
Enzyme Sequence MAVASRKLGALVLVAVLCLSLPTGCLSSQQAAALFIFGDSVFDPGNNNHINTHVNFKANFWPYGQSYFSSPTGRFSDGRIIPDFIAEYASLPIIPAYLEPNNDFTHGANFASAGAGALIASHAGLAVGLQTQLRYFGDLVDHYRQNLGDIKSRQLLSDAVYLFSCGGNDYQSPYYPYTQEQYVDIVIGNMTNVIKGIYEKGGRKFGVVNVPLIGCWPGMRAKQPGNTCNTEVDELTRLHNQAFAKRLEQLEKQLEGFVYAKFDLSTAILNRMKNPSKYGFKEGESACCGSGPFGGNYDCGRIKEFGLCDNATEYFFFDPFHPNELASRQFAEMFWDGDSMVTQPYNLKALFEGKPSTKYLPNDEL
Enzyme Length 365
Uniprot Accession Number H6U1I8
Absorption
Active Site ACT_SITE 40; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q09LX1; ACT_SITE 318; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q09LX1; ACT_SITE 321; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q09LX1
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=(1R,3R)-chrysanthemoyl-CoA + (Z,S)-pyrethrolone = CoA + pyrethrin I; Xref=Rhea:RHEA:60744, ChEBI:CHEBI:27815, ChEBI:CHEBI:39111, ChEBI:CHEBI:57287, ChEBI:CHEBI:143950; Evidence={ECO:0000269|PubMed:22385412};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60745; Evidence={ECO:0000269|PubMed:22385412}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-pyrethroyl-CoA + (Z,S)-pyrethrolone = CoA + pyrethrin II; Xref=Rhea:RHEA:60748, ChEBI:CHEBI:27474, ChEBI:CHEBI:39111, ChEBI:CHEBI:57287, ChEBI:CHEBI:143953; Evidence={ECO:0000269|PubMed:22385412};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60749; Evidence={ECO:0000269|PubMed:22385412}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-chrysanthemoyl-CoA + (Z,S)-jasmololone = CoA + jasmolin I; Xref=Rhea:RHEA:60752, ChEBI:CHEBI:39113, ChEBI:CHEBI:57287, ChEBI:CHEBI:143950, ChEBI:CHEBI:143951; Evidence={ECO:0000269|PubMed:22385412};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60753; Evidence={ECO:0000269|PubMed:22385412}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-chrysanthemoyl-CoA + (Z,S)-cinerolone = cinerin I + CoA; Xref=Rhea:RHEA:60756, ChEBI:CHEBI:3706, ChEBI:CHEBI:57287, ChEBI:CHEBI:143950, ChEBI:CHEBI:143952; Evidence={ECO:0000269|PubMed:22385412};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60757; Evidence={ECO:0000269|PubMed:22385412}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-pyrethroyl-CoA + (Z,S)-jasmololone = CoA + jasmolin II; Xref=Rhea:RHEA:60760, ChEBI:CHEBI:39114, ChEBI:CHEBI:57287, ChEBI:CHEBI:143951, ChEBI:CHEBI:143953; Evidence={ECO:0000269|PubMed:22385412};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60761; Evidence={ECO:0000269|PubMed:22385412}; CATALYTIC ACTIVITY: Reaction=(1R,3R)-pyrethroyl-CoA + (Z,S)-cinerolone = cinerin II + CoA; Xref=Rhea:RHEA:60764, ChEBI:CHEBI:3707, ChEBI:CHEBI:57287, ChEBI:CHEBI:143952, ChEBI:CHEBI:143953; Evidence={ECO:0000269|PubMed:22385412};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60765; Evidence={ECO:0000269|PubMed:22385412};
DNA Binding
EC Number 3.1.1.-
Enzyme Function FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide (PubMed:30468448). Acyltransferase that catalyzes the esterification of terpene acids and lipid alcohol substrates into pyrethrins; mediates the transfer of a chrysanthemoyl moiety from the coenzyme A (CoA) thio-ester chrysanthemoyl CoA to pyrethrolone, and, to a lower extent, to jasmololone and cinerolone thus producing pyrethrins (e.g. pyrethrin type I) (PubMed:22385412). Can also use pyrethroyl CoA as substrate (PubMed:22385412). Has also esterase activity, being able to cleave the ester bond of pyrethrin I, p-nitrophenyl butanoate and p-nitrophenyl octanoate to produce pyrethrolone and p-nitrophenol, respectively (PubMed:22385412). {ECO:0000269|PubMed:22385412, ECO:0000303|PubMed:30468448}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius. {ECO:0000269|PubMed:22385412};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:22385412};
Pathway PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:22385412}.
nucleotide Binding
Features Active site (3); Chain (1); Glycosylation (2); Mutagenesis (1); Sequence conflict (11); Signal peptide (1); Site (2)
Keywords Direct protein sequencing;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Secreted;Signal
Interact With
Induction INDUCTION: By wounding. {ECO:0000269|PubMed:22385412}.
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:22385412}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..27; /evidence=ECO:0000269|PubMed:22385412
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 40,378
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=768 uM for (1R,3R)-chrysanthemoyl CoA (in the presence of (S)-pyrethrolone, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; KM=30.7 uM for (S)-pyrethrolone (in the presence of (1R,3R)-chrysanthemoyl CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; KM=1050 uM for (1R,3R)-pyrethroyl CoA (in the presence of (S)-pyrethrolone, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; KM=31.7 uM for (S)-pyrethrolone (in the presence of (1R,3R)-pyrethroyl CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=1.52 nmol/sec/mg enzyme with (1R,3R)-chrysanthemoyl CoA as substrate (in the presence of (S)-pyrethrolone, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.95 nmol/sec/mg enzyme with (1R,3R)-pyrethroyl CoA as substrate (in the presence of (S)-pyrethrolone, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=1.17 nmol/sec/mg enzyme with (S)-pyrethrolone as substrate (in the presence of (1R,3R)-chrysanthemoyl CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.65 nmol/sec/mg enzyme with (S)-pyrethrolone as substrate (in the presence of (1R,3R)-pyrethroyl CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.0105 nmol/sec/mg enzyme with pyrethrin I as substrate (in the absence of CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.0305 nmol/sec/mg enzyme with pyrethrin I as substrate (in the presence of CoA, at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.88 nmol/sec/mg enzyme with p-nitrophenyl butanoate as substrate (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412}; Vmax=0.309 nmol/sec/mg enzyme with p-nitrophenyl octanoate as substrate (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22385412};
Metal Binding
Rhea ID RHEA:60744; RHEA:60745; RHEA:60748; RHEA:60749; RHEA:60752; RHEA:60753; RHEA:60756; RHEA:60757; RHEA:60760; RHEA:60761; RHEA:60764; RHEA:60765
Cross Reference Brenda