| IED ID | IndEnz0005001092 |
| Enzyme Type ID | lipase001092 |
| Protein Name |
NADPH-dependent 1-acyldihydroxyacetone phosphate reductase ADR EC 1.1.1.101 1-acyl DHAP reductase Acyl/alkyl DHAP reductase Acylglycerone-phosphate reductase Triacylglycerol lipase AYR1 TAG lipase EC 3.1.1.3 |
| Gene Name | AYR1 GBG1 YIL124W |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSELQSQPKKIAVVTGASGGIGYEVTKELARNGYLVYACARRLEPMAQLAIQFGNDSIKPYKLDISKPEEIVTFSGFLRANLPDGKLDLLYNNAGQSCTFPALDATDAAVEQCFKVNVFGHINMCRELSEFLIKAKGTIVFTGSLAGVVSFPFGSIYSASKAAIHQYARGLHLEMKPFNVRVINAITGGVATDIADKRPLPETSIYNFPEGREAFNSRKTMAKDNKPMPADAYAKQLVKDILSTSDPVDVYRGTFANIMRFVMIFVPYWLLEKGLSKKFKLDKVNNALKSKQKNKDD |
| Enzyme Length | 297 |
| Uniprot Accession Number | P40471 |
| Absorption | |
| Active Site | ACT_SITE 18; /note=Nucleophile; for lipase activity; /evidence=ECO:0000305|PubMed:24187129; ACT_SITE 157; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10001 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by divalent cations and N-ethylmaleimide. Activity is reduced under anaerobic growth conditions. {ECO:0000269|PubMed:1512203}. |
| Binding Site | BINDING 144; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1-acylglycerone 3-phosphate + H(+) + NADPH = a 1-acyl-sn-glycero-3-phosphate + NADP(+); Xref=Rhea:RHEA:33375, ChEBI:CHEBI:15378, ChEBI:CHEBI:57534, ChEBI:CHEBI:57783, ChEBI:CHEBI:57970, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:10617610};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33376; Evidence={ECO:0000305|PubMed:10617610}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + NADP(+) = 1-hexadecanoylglycerone 3-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:17341, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:57783, ChEBI:CHEBI:58303, ChEBI:CHEBI:58349; EC=1.1.1.101; Evidence={ECO:0000269|PubMed:1512203}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:24187129};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000305|PubMed:24187129}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:24187129};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:24187129}; |
| DNA Binding | |
| EC Number | 1.1.1.101; 3.1.1.3 |
| Enzyme Function | FUNCTION: Can convert acyl and alkyl dihydroxyacetone-phosphate (DHAP) into glycerolipids and ether lipids, respectively. Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA) (PubMed:1512203, PubMed:10617610). Also has triacylglycerol (TAG) lipase activity. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs (PubMed:24187129). Required for spore germination (PubMed:10617610). Plays a role in cell wall biogenesis, but this effect may be indirect by affecting the activities of cell wall synthesis enzymes (PubMed:23956635). Lipolysis of TAG by AYR1 is essential for starvation-induced autophagy (PubMed:26162625). Forms an NADPH-regulated cation-selective channel in the mitochondrial outer membrane (PubMed:28916712). {ECO:0000269|PubMed:10617610, ECO:0000269|PubMed:1512203, ECO:0000269|PubMed:23956635, ECO:0000269|PubMed:24187129, ECO:0000269|PubMed:26162625, ECO:0000269|PubMed:28916712}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. Thermostable for 10 min up to 45 degrees Celsius. {ECO:0000269|PubMed:1512203}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.7-7.2. {ECO:0000269|PubMed:1512203}; |
| Pathway | |
| nucleotide Binding | NP_BIND 13..21; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q92506; NP_BIND 63..65; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q92506; NP_BIND 157..161; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q92506; NP_BIND 190..192; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q92506 |
| Features | Active site (2); Binding site (1); Chain (1); Motif (1); Mutagenesis (1); Nucleotide binding (4) |
| Keywords | Direct protein sequencing;Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Membrane;Mitochondrion;Mitochondrion outer membrane;NAD;NADP;Oxidoreductase;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Expressed during vegetative growth with a maximum level of transcription at G1 phase, after which it is decreased during the remainder of the cell cycle. {ECO:0000269|PubMed:23956635}. |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:10617610, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093}. Mitochondrion outer membrane {ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:28916712}. Endoplasmic reticulum {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:28916712}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10998572; 11274415; 11283351; 11805837; 12087109; 12112241; 15780652; 16330752; 16919863; 18467557; 18719252; 19536198; 19696439; 20231294; 21146236; 22345606; 23027642; 23202731; 23275493; 23631861; 24007978; 24520995; 24597968; 24628496; 24678285; 25483081; 25894691; 27637775; 7897322; |
| Motif | MOTIF 16..20; /note=GXSXG; /evidence=ECO:0000305|PubMed:24187129 |
| Gene Encoded By | |
| Mass | 32,814 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for NADPH {ECO:0000269|PubMed:1512203}; KM=15 uM for hexadecyl dihydroxyacetone-phosphate {ECO:0000269|PubMed:1512203}; KM=3.5 mM for p-nitrophenylacetate {ECO:0000269|PubMed:24187129}; KM=1.52 mM for p-nitrophenylbutyrate {ECO:0000269|PubMed:24187129}; KM=61.21 uM for 1,2,3-tri-(9Z-octadecenoyl)-glycerol {ECO:0000269|PubMed:24187129}; Vmax=3.8 nmol/min/mg enzyme for hexadecyl dihydroxyacetone-phosphate {ECO:0000269|PubMed:1512203}; Vmax=18.5 umol/min/mg enzyme for p-nitrophenylacetate {ECO:0000269|PubMed:24187129}; Vmax=14.06 umol/min/mg enzyme for p-nitrophenylbutyrate {ECO:0000269|PubMed:24187129}; Vmax=10.93 pmol/h/mg enzyme for 1,2,3-tri-(9Z-octadecenoyl)-glycerol {ECO:0000269|PubMed:24187129}; |
| Metal Binding | |
| Rhea ID | RHEA:33375; RHEA:33376; RHEA:17341; RHEA:12044; RHEA:12045; RHEA:38575; RHEA:38576 |
| Cross Reference Brenda |