| IED ID | IndEnz0005001337 |
| Enzyme Type ID | lipase001337 |
| 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 |