| IED ID | IndEnz0005000527 |
| Enzyme Type ID | lipase000527 |
| Protein Name |
Caffeoylshikimate esterase EC 3.1.1.- Lysophospholipase 2 LysoPL2 |
| Gene Name | CSE At1g52760 F14G24.3 |
| 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 | MPSEAESSANSAPATPPPPPNFWGTMPEEEYYTSQGVRNSKSYFETPNGKLFTQSFLPLDGEIKGTVYMSHGYGSDTSWMFQKICMSFSSWGYAVFAADLLGHGRSDGIRCYMGDMEKVAATSLAFFKHVRCSDPYKDLPAFLFGESMGGLVTLLMYFQSEPETWTGLMFSAPLFVIPEDMKPSKAHLFAYGLLFGLADTWAAMPDNKMVGKAIKDPEKLKIIASNPQRYTGKPRVGTMRELLRKTQYVQENFGKVTIPVFTAHGTADGVTCPTSSKLLYEKASSADKTLKIYEGMYHSLIQGEPDENAEIVLKDMREWIDEKVKKYGSKTA |
| Enzyme Length | 332 |
| Uniprot Accession Number | Q9C942 |
| Absorption | |
| Active Site | ACT_SITE 147; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 268; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 298; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=5-O-[(E)-caffeoyl]-shikimate + H2O = (E)-caffeate + H(+) + shikimate; Xref=Rhea:RHEA:49264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:36208, ChEBI:CHEBI:57770, ChEBI:CHEBI:91005; Evidence={ECO:0000269|PubMed:23950498}; |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Esterase involved in the biosynthesis of lignin. Hydrolyzes caffeoylshikimate into caffeate and shikimate. Together with 4-coumarate--CoA ligase (4CL), acts on an alternative reaction for the formation of caffeoyl-CoA and bypasses the second reaction of shikimate O-hydroxycinnamoyltransferase (HST). Accepts also 4-coumaroylshikimate as substrate, but with lower activity. According to PubMed:20345607 and PubMed:22915575, posseses monoacylglycerol O-acyltransferase, monoacylglycerol lipase and lysophospholipase activities in vitro. With the association of ACBP2, may promote the degradation of lysophosphatidylcholine and detoxify the peroxidized membrane in response to cadmium-induced oxidative stress. However these results require additional confirmation in vivo. {ECO:0000269|PubMed:20345607, ECO:0000269|PubMed:20657176, ECO:0000269|PubMed:22915575, ECO:0000269|PubMed:23950498}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Region (1) |
| Keywords | Cell membrane;Hydrolase;Lignin biosynthesis;Membrane;Reference proteome |
| Interact With | |
| Induction | INDUCTION: By zinc and H(2)O(2). {ECO:0000269|PubMed:20345607}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:20345607}; Peripheral membrane protein {ECO:0000305|PubMed:20345607}. Note=Colocalizes with ACBP2. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 13677466; 16132859; 16829591; 18650403; 23505340; 26932457; 27037613; 27390589; 28878037; 30782848; 31040279; |
| Motif | |
| Gene Encoded By | |
| Mass | 36,975 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=96.5 uM for caffeoylshikimate {ECO:0000269|PubMed:20345607, ECO:0000269|PubMed:23950498}; KM=211 uM for 4-coumarylshikimate {ECO:0000269|PubMed:20345607, ECO:0000269|PubMed:23950498}; KM=6.6 uM for lysophosphatidylcholine (at pH 8.0 and 33 degrees Celsius) {ECO:0000269|PubMed:20345607, ECO:0000269|PubMed:23950498}; Vmax=9.3 pmol/sec/mg enzyme toward caffeoylshikimate {ECO:0000269|PubMed:20345607, ECO:0000269|PubMed:23950498}; Vmax=0.66 pmol/sec/mg enzyme toward 4-coumarylshikimate {ECO:0000269|PubMed:20345607, ECO:0000269|PubMed:23950498}; Vmax=0.030 umol/min/mg enzyme toward lysophosphatidylcholine (at pH 8.0 and 33 degrees Celsius) {ECO:0000269|PubMed:20345607, ECO:0000269|PubMed:23950498}; |
| Metal Binding | |
| Rhea ID | RHEA:49264 |
| Cross Reference Brenda |