3.5.1.48: acetylspermidine deacetylase
This is an abbreviated version!
For detailed information about acetylspermidine deacetylase, go to the full flat file.
Word Map on EC 3.5.1.48
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3.5.1.48
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deacetylases
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deacetylation
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hdac11
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mycoplana
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ramosa
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pharmacology
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drug development
- 3.5.1.48
- deacetylases
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deacetylation
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hdac11
- mycoplana
- ramosa
- pharmacology
- drug development
Reaction
Synonyms
acetylpolyamine amidohydrolase, APAH, HDAC10, histone deacetylase 10, N1-acetylspermidine amidohydrolase, N1-acetylspermidine deacetylase, N8-acetyl-monoacetylspermidine deacetylase, N8-acetylspermidine deacetylase, polyamine deacetylase, zHDAC10
ECTree
3.5.1.48 acetylspermidine deacetylaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.5.1.48 - acetylspermidine deacetylase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
diacetylspermidine + H2O
acetate + spermidine
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81.9% activity of that of N8-acetylspermidine
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?
N-(3-aminopropyl)acetamide + H2O
propane-1,3-diamine + acetate
very low activity
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-
?
N1,N8-diacetylspermidine + 2 H2O
2 acetate + spermidine
moderate activity
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-
?
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin + H2O
?
very low activity
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-
?
7-(Nalpha-acetyl-glycyl-L-alanyl-Nepsilon-acetyl-L-lysyl)amino-4-methylcoumarin + H2O
?
low activity
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-
?
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin + H2O
?
very low activity
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-
?
7-(Nalpha-acetyl-L-arginyl-glycyl-Nepsilon-acetyl-L-lysyl)-amino-4-methylcoumarin + H2O
?
low activity
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-
?
N-(8-aminooctyl)acetamide + H2O
octane-1,8-diamine + acetate
moderate to high activity
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-
?
N-(8-aminooctyl)acetamide + H2O
octane-1,8-diamine + acetate
moderate activity
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-
?
N8-acetylspermidine + H2O
acetate + spermidine
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involvement in cell growth and differentiation
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?
N8-acetylspermidine + H2O
acetate + spermidine
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involvement in controlling the levels of polyamines and acetylated polyamines in tissues
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?
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide + H2O
?
low activity
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-
?
Nalpha-acetyl-L-alanyl-Nepsilon-acetyl-L-lysyl-L-alaninamide + H2O
?
low activity
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?
additional information
?
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histone deacetylase 10 (HDAC10) from Danio rerio is a highly specific N8-acetylspermidine deacetylase. No activity with N1-acetylspermidine and N1-acetylspermine
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?
additional information
?
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histone deacetylase 10 (HDAC10) from Danio rerio is a highly specific N8-acetylspermidine deacetylase. No activity with N1-acetylspermidine and N1-acetylspermine
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-
?
additional information
?
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zebrafish HDAC10 complexed with a transition-state analogue inhibitor reveals that a glutamate gatekeeper and a sterically constricted active site confer specificity for N8-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. The N4 amino group of N8-acetylspermidine is recognized by a direct hydrogen bond with E117. No activity with TK(ac)PIW, AK(ac)P, GAK(ac), AK(ac), AK(ac)A, K(ac)NL, K(ac)NL, and GAK(ac)NLQ
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-
?
additional information
?
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zebrafish HDAC10 complexed with a transition-state analogue inhibitor reveals that a glutamate gatekeeper and a sterically constricted active site confer specificity for N8-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. The N4 amino group of N8-acetylspermidine is recognized by a direct hydrogen bond with E117. No activity with TK(ac)PIW, AK(ac)P, GAK(ac), AK(ac), AK(ac)A, K(ac)NL, K(ac)NL, and GAK(ac)NLQ
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-
?
additional information
?
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histone deacetylase 10 (HDAC10) from Homo sapiens is a highly specific N8-acetylspermidine deacetylase. No activity with N1-acetylspermidine and N1-acetylspermine
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-
?
additional information
?
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histone deacetylase 10 (HDAC10) from Homo sapiens is a highly specific N8-acetylspermidine deacetylase. No activity with N1-acetylspermidine and N1-acetylspermine
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-
?
additional information
?
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the conserved glutamate gatekeeper and a sterically constricted active site confer specificity for N8-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. Analysis of the intermolecular interactions of N8-acetylspermidine in the active site of hHDAC10 based on the structure of the Danio rerio enzyme-inhibitor crystal structure zHDAC10-AAT complex. No activity with N-(3-aminopropyl)acetamide, TK(ac)PIW, AK(ac)P, GAK(ac), AK(ac), K(ac)NL, K(ac)NL, and GAK(ac)NLQ
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-
?
additional information
?
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the conserved glutamate gatekeeper and a sterically constricted active site confer specificity for N8-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. Analysis of the intermolecular interactions of N8-acetylspermidine in the active site of hHDAC10 based on the structure of the Danio rerio enzyme-inhibitor crystal structure zHDAC10-AAT complex. No activity with N-(3-aminopropyl)acetamide, TK(ac)PIW, AK(ac)P, GAK(ac), AK(ac), K(ac)NL, K(ac)NL, and GAK(ac)NLQ
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?
additional information
?
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the bacterial enzyme from Mycoplana ramosa has broader substrate specificity in comparison with mammalian enzyme. Its substrates include both small and large acetylpolyamines such as acetylputrescine, acetylcadaverine, N1- and N8-acetylspermidine, and N1-acetylspermine
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?
additional information
?
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usage of the commercially available Fluor-de-Lys deacetylase fluorogenic substrate fir enzyme activity assays
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?
