Detail Information for IndEnz0005001236
IED ID IndEnz0005001236
Enzyme Type ID lipase001236
Protein Name Cardiolipin-specific deacylase 1, mitochondrial
EC 3.5.1.-
Gene Name CLD1 YGR110W G6140
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 MFKSTLNSIIRRPLKGFQLLRGADSSNTRPQSPRASARDVTEKQILRTPSAPTAIPLREIIYRVPSLFPRPLEDSVKDFRDFIKNEDAFQTELLKTLPFYPTPSESKTARLIRTVVDDEGNYINEFCIRPRKTSVPEADLKHLVFIHGYGAGLGFFIKNFEDIPLLDNEWCIHAIDLPGYGFSSRPKFPFEYPRDNIHSVQDWFHERIHTWFSKRNLLNRPEKNIVMAHSLGSYLMALYLQKYKESPSFKKLILCSPAGVSYRDFNNTASEVEKWKPPPWWYVKLWDRNISPFTLVRNFRQLGSKITSGWSYRRFKHILNGDPEQSKRFEALHRYAYAIFNKRGSGEYLLSFALKCGGEPRLSLEQQLFDGKKSDILKNSNCDWLWLYGDDDWMDVNGGLRVSRFLKEKLKQKSNVIIVPHSGHHLYLDNYKFFNNILTKEMQKI
Enzyme Length 445
Uniprot Accession Number P53264
Absorption
Active Site ACT_SITE 230; /note=Nucleophile; /evidence=ECO:0000269|PubMed:23637464; ACT_SITE 392; /note=Charge relay system; /evidence=ECO:0000269|PubMed:23637464; ACT_SITE 424; /note=Charge relay system; /evidence=ECO:0000269|PubMed:23637464
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a cardiolipin + H2O = 1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol + a fatty acid + H(+); Xref=Rhea:RHEA:32935, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:62237, ChEBI:CHEBI:64743; Evidence={ECO:0000269|PubMed:19244244, ECO:0000269|PubMed:24318983, ECO:0000269|PubMed:27982579};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32936; Evidence={ECO:0000305|PubMed:19244244, ECO:0000305|PubMed:24318983, ECO:0000305|PubMed:27982579};
DNA Binding
EC Number 3.5.1.-
Enzyme Function FUNCTION: Mitochondrial cardiolipin-specific phospholipase which deacylates de novo synthesized cardiolipin (CL). Part of the remodeling process of cardiolipin, which involves deacylation-reacylation of premature cardiolipin. Has a strong substrate preference for palmitic acid residues and generates monolysocardiolipin (MLCL) for TAZ1-dependent reacylation with unsaturated fatty acids (PubMed:19244244, PubMed:23637464). The hydrolytic selectivity of the enzyme toward C16-CL substrates contributes to the preservation of C18:1-containing CL species (PubMed:27982579). Has high specificity towards peroxidized cardiolipids CL(OX). Required to mitigate oxidative stress by removing CL(OX) (PubMed:29935382). {ECO:0000269|PubMed:19244244, ECO:0000269|PubMed:23637464, ECO:0000269|PubMed:27982579, ECO:0000269|PubMed:29935382}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Compositional bias (1); Domain (1); Motif (2); Mutagenesis (5); Region (1); Transit peptide (1)
Keywords Hydrolase;Membrane;Mitochondrion;Mitochondrion inner membrane;Reference proteome;Transferase;Transit peptide
Interact With
Induction INDUCTION: Expressed in aerobic conditions and under genotoxic stress (PubMed:10601195, PubMed:15878181). Expression is increased during respiratory growth and regulated by the heme activator protein transcriptional activation complex (PubMed:24318983). {ECO:0000269|PubMed:10601195, ECO:0000269|PubMed:15878181, ECO:0000269|PubMed:24318983}.
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19244244}. Mitochondrion inner membrane {ECO:0000269|PubMed:23637464}; Peripheral membrane protein {ECO:0000269|PubMed:23637464}; Matrix side {ECO:0000269|PubMed:23637464}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11283351; 14690591; 17630978; 18202368; 19536198; 20818735; 21912624; 22345606; 24007978; 24184646; 24190879; 24220496; 24285538; 24520995; 24678285; 24926745; 25432572; 26819558; 27402848; 27502688;
Motif MOTIF 228..232; /note=GXSXG lipase motif; /evidence=ECO:0000305|PubMed:19244244; MOTIF 424..429; /note=HXXXXD acyl transferase motif; /evidence=ECO:0000305|PubMed:19244244
Gene Encoded By
Mass 52,045
Kinetics
Metal Binding
Rhea ID RHEA:32935; RHEA:32936
Cross Reference Brenda