UniProt ID: A0A8M9PY99 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. SIMILARITY: Belongs to the histone deacetylase family. HD type 2 subfamily. {ECO:0000256|ARBA:ARBA00007738}. |
UniProt ID: F1QCV2 |
FUNCTION: Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine (PubMed:28516954). Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine (PubMed:28516954). Has a very weak lysine deacetylase, if any (PubMed:28516954). {ECO:0000269|PubMed:28516954}. CATALYTIC ACTIVITY: Reaction=H2O + N(8)-acetylspermidine = acetate + spermidine; Xref=Rhea:RHEA:23928, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57834, ChEBI:CHEBI:58535; EC=3.5.1.48; Evidence={ECO:0000269|PubMed:28516954}; CATALYTIC ACTIVITY: Reaction=H2O + N-acetylputrescine = acetate + putrescine; Xref=Rhea:RHEA:23412, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:58263, ChEBI:CHEBI:326268; EC=3.5.1.62; Evidence={ECO:0000269|PubMed:28516954}; CATALYTIC ACTIVITY: Reaction=H2O + N-acetylcadaverine = acetate + cadaverine; Xref=Rhea:RHEA:51892, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:58384, ChEBI:CHEBI:134408; Evidence={ECO:0000269|PubMed:28516954}; BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=90 uM for acetylcadaverine {ECO:0000269|PubMed:28516954}; KM=160 uM for acetylputrescine {ECO:0000269|PubMed:28516954}; KM=130 uM for N(8)-acetylspermidine {ECO:0000269|PubMed:28516954}; KM=180 uM for N(1),N(8)-diacetylspermidine {ECO:0000269|PubMed:28516954}; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969S8}. Nucleus {ECO:0000250|UniProtKB:Q969S8}. Note=Excluded from the nucleoli. {ECO:0000250|UniProtKB:Q969S8}. SIMILARITY: Belongs to the histone deacetylase family. HD type 2 subfamily. {ECO:0000305}. CAUTION: Originally thought to be a histone deacetylase and shown in vitro to have this activity (By similarity). Has also been shown to be involved in MSH2 deacetylation (By similarity). However, protein deacetylase activity is a matter of debate, as 3D structure analysis shows that a glutamate gatekeeper and a sterically constricted active site confer specificity for N(8)-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. Supporting this observation, has been shown to exhibit only very low activity, if any, towards acetyl- lysine peptide substrates (By similarity). {ECO:0000250|UniProtKB:Q969S8}. |
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