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Cell Reactant:Histone deacetylase 8 (HDAC8)
Syringe Reactant:BDBM50005711
Meas. Tech.:Enzyme Inhibition
Entry Date:09/14/15
 
ΔG°:-36±1 (kJ/mole)
pH:7.5±0
Log10Kb:6.53± n/a
Temperature:25±0 (K)
ΔH° :-36.9± (kJ/mole)
ΔHobs :-37.4±2 (kJ/mole)
Ionic Strength:n/a
Corrected for ΔHioniz:n/a
Protons Released:n/a
ΔCp :n/a
Stoich. Param.:n/a
ΔS° : -0.003±0.00100 (kJ/mole-K)
Comments:n/a
 
Citation Singh, RKSuzuki, TMandal, TBalsubramanian, NHaldar, MMueller, DJStrode, JACook, GMallik, SSrivastava, DK Thermodynamics of binding of structurally similar ligands to histone deacetylase 8 sheds light on challenges in the rational design of potent and isozyme-selective inhibitors of the enzyme. Biochemistry53:7445-58 (2014) [PubMed]  Article
More Info.:  Get all data from this article ,  ITC RUN data ,  Solution Info ,  Instrument Info
 
Histone deacetylase 8 (HDAC8)
Source:n/a
Purity:n/a
Prep. Method:n/a
Name:Histone deacetylase 8
Synonyms:HD8 | HDAC8 | HDAC8_HUMAN | HDACL1 | Histone deacetylase 8 (HDAC-8) | Human HDAC8
Type:Enzyme
Mol. Mass.:41749.60
Organism:Homo sapiens (Human)
Description:Q9BY41
Residue:377
Sequence:
MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPK
VASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATI
TAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLH
HGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKY
YQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLI
LGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPH
RIQQILNYIKGNLKHVV
Blast this sequence in BindingDB or PDB
  Blast E-value cutoff:
BDBM50005711
Source:n/a
Purity:n/a
Prep. Method:n/a
NameBDBM50005711
Synonyms:CHEBI:46024 | GNF-Pf-1011 | TRICHOSTATIN | Trichostatin A | Trichostatin A (TSA) | US10011611, Trichostatin A | US10722597, Compound Trichostatin | US11535598, Compound Trichostatin A | US20230322747, Compound trichostatin A | US9265734, TSA
TypeSmall organic molecule
Emp. Form.C17H22N2O3
Mol. Mass.302.3682
SMILESC[C@H](\C=C(/C)\C=C\C(=O)NO)C(=O)c1ccc(cc1)N(C)C |r|
Structure
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