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UniProt functional annotation for Q48935 | ||
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| UniProt code: Q48935. |
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| Organism: | |
Mycoplana ramosa (Mycoplana bullata). |
| Taxonomy: | |
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae; Mycoplana. |
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| Function: | |
Involved in polyamine metabolism. Catalyzes the deacetylation of various acetylated polyamines such as N-acetylputrescine, N- acetylcadaverine, N(1)-acetylspermine, N(1)-acetylspermidine and N(8)- acetylspermidine (PubMed:8824626, PubMed:3207420). In vitro, is also able to deacetylate L-Lys(epsilon-acetyl)coumarin, but has very low activity towards the larger tetrapeptide N-acetyl-L-Arg-L-His-L- Lys(epsilon-acetyl)-L-Lys(epsilon-acetyl)coumarin (PubMed:21268586). {ECO:0000269|PubMed:21268586, ECO:0000269|PubMed:3207420, ECO:0000269|PubMed:8824626}. |
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| 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:3207420, ECO:0000269|PubMed:8824626}; |
| 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:3207420, ECO:0000269|PubMed:8824626}; |
| Catalytic activity: | |
Reaction=H2O + N(1)-acetylspermine = acetate + spermine; Xref=Rhea:RHEA:51896, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:45725, ChEBI:CHEBI:58101; Evidence={ECO:0000269|PubMed:3207420, ECO:0000269|PubMed:8824626}; |
| Catalytic activity: | |
Reaction=H2O + N(1)-acetylspermidine = acetate + spermidine; Xref=Rhea:RHEA:51900, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57834, ChEBI:CHEBI:58324; Evidence={ECO:0000269|PubMed:3207420, ECO:0000269|PubMed:8824626}; |
| 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:3207420, ECO:0000269|PubMed:8824626}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:21268586, ECO:0000269|PubMed:8824626, ECO:0000305|PubMed:3207420}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:21268586, ECO:0000269|PubMed:26200446, ECO:0000269|PubMed:3207420, ECO:0000269|PubMed:8824626}; |
| Activity regulation: | |
Zinc ions inhibit enzyme activity in a dose- dependent manner (PubMed:8824626). Inhibited by KCl at concentrations above 10 mM (PubMed:21268586). Inhibited by o-oxyquinoline in vitro, suggesting that it is a metalloprotein (PubMed:3207420). Inhibited by various substrate N(8)-acetylspermidine analogs bearing different metal-binding groups such as trifluoromethylketone, thiol, or hydroxamate, and by hydroxamate analogs of short-chain acetyldiamines (PubMed:26200446). {ECO:0000269|PubMed:21268586, ECO:0000269|PubMed:26200446, ECO:0000269|PubMed:3207420, ECO:0000269|PubMed:8824626}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=50 uM for N-acetylcadaverine {ECO:0000269|PubMed:8824626}; KM=220 uM for N-acetylputrescine {ECO:0000269|PubMed:8824626}; KM=130 uM for N(1)-acetylspermidine {ECO:0000269|PubMed:8824626}; KM=310 uM for N(8)-acetylspermidine {ECO:0000269|PubMed:8824626}; KM=290 uM for N(1)-acetylspermine {ECO:0000269|PubMed:8824626}; Vmax=27 umol/min/mg enzyme with N-acetylcadaverine as substrate {ECO:0000269|PubMed:8824626}; Vmax=27 umol/min/mg enzyme with N-acetylputrescine as substrate {ECO:0000269|PubMed:8824626}; Vmax=16.5 umol/min/mg enzyme with N(1)-acetylspermidine as substrate {ECO:0000269|PubMed:8824626}; Vmax=17.2 umol/min/mg enzyme with N(8)-acetylspermidine as substrate {ECO:0000269|PubMed:8824626}; Vmax=13.4 umol/min/mg enzyme with N(1)-acetylspermine as substrate {ECO:0000269|PubMed:8824626}; pH dependence: Optimum pH is 9 with acetylputrescine, N(1)-acetylspermidine, and N(8)-acetylspermidine as substrates, and is 8 with acetylcadaverine as substrate. {ECO:0000269|PubMed:3207420}; |
| Pathway: | |
Amine and polyamine metabolism. {ECO:0000305|PubMed:8824626}. |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:21268586, ECO:0000269|PubMed:3207420}. |
| Similarity: | |
Belongs to the histone deacetylase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.