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Literature summary extracted from

  • Vannini, A.; Volpari, C.; Filocamo, G.; Casavola, E.C.; Brunetti, M.; Renzoni, D.; Chakravarty, P.; Paolini, C.; De Francesco, R.; Gallinari, P.; Steinkuhler, C.; Di Marco, S.
    Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor (2004), Proc. Natl. Acad. Sci. USA, 101, 15064-15069.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.5.1.98 medicine knock-down of isoform HDAC8 expression by RNAi inhibits growth of human lung, colon, and cervical cancer cell lines Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.98
-
 Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.98 molecular modeling of isoform HDAC8 in complex with inhibitor N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.98 additional information knock-down of isoform HDAC8 expression by RNAi inhibits growth of human lung, colon, and cervical cancer cell lines Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.98 apicidin
-
 Homo sapiens
3.5.1.98 N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
-
 Homo sapiens
3.5.1.98 pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate i.e. MS27-275 Homo sapiens
3.5.1.98 suberoylanilide hydroxamic acid
-
 Homo sapiens
3.5.1.98 trichostatin A
-
 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.98 K+ presence of two potassium ions in the structure of isoform HDAC8, one of which interacts with the key catalytic residues. Direct role of potassium in fold stabilization Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.98 Homo sapiens Q9BY41 isoforms HDAC1, HDAC3, HDAC8
-

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.5.1.98 0.0000006
-
 isoform HDAC3 Homo sapiens trichostatin A
3.5.1.98 0.0000007
-
 isoform HDAC3 Homo sapiens apicidin
3.5.1.98 0.0000015
-
 isoform HDAC1 Homo sapiens trichostatin A
3.5.1.98 0.000002
-
 isoform HDAC1 Homo sapiens apicidin
3.5.1.98 0.000044
-
 isoform HDAC3 Homo sapiens N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
3.5.1.98 0.000086
-
 isoform HDAC1 Homo sapiens N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
3.5.1.98 0.000106
-
 isoform HDAC3 Homo sapiens suberoylanilide hydroxamic acid
3.5.1.98 0.000119
-
 isoform HDAC1 Homo sapiens suberoylanilide hydroxamic acid
3.5.1.98 0.000175
-
 isoform HDAC8 Homo sapiens N-hydroxy-4-(methyl[(5-pyridin-2-yl-2-thienyl)sulfonyl]amino)benzamide
3.5.1.98 0.000185
-
 isoform HDAC1 Homo sapiens pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
3.5.1.98 0.000201
-
 isoform HDAC3 Homo sapiens pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate
3.5.1.98 0.00049
-
 isoform HDAC8 Homo sapiens trichostatin A
3.5.1.98 0.001
-
 isoform HDAC8 Homo sapiens apicidin
3.5.1.98 0.004
-
 isoform HDAC8 Homo sapiens suberoylanilide hydroxamic acid
3.5.1.98 0.01
-
 isoform HDAC8 Homo sapiens pyridin-3-ylmethyl (4-[[(2-aminophenyl)amino]carbonyl]benzyl)carbamate