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Information on EC 3.5.1.98 - histone deacetylase

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.98 histone deacetylase
IUBMB Comments
A class of enzymes that remove acetyl groups from N6-acetyl-lysine residues on a histone. The reaction of this enzyme is opposite to that of EC 2.3.1.48, histone acetyltransferase. Histone deacetylases (HDACs) can be organized into three classes, HDAC1, HDAC2 and HDAC3, depending on sequence similarity and domain organization. Histone acetylation plays an important role in regulation of gene expression. In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation . May be identical to EC 3.5.1.17, acyl-lysine deacylase.
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UNIPROT: O67135
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
Synonyms
histone deacetylase, hdac1, hdac6, hdac2, hdac3, hdac4, hdac5, hdac8, hdac9, hdac7, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
histone deacetylase-like protein
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SYSTEMATIC NAME
IUBMB Comments
histone amidohydrolase
A class of enzymes that remove acetyl groups from N6-acetyl-lysine residues on a histone. The reaction of this enzyme is opposite to that of EC 2.3.1.48, histone acetyltransferase. Histone deacetylases (HDACs) can be organized into three classes, HDAC1, HDAC2 and HDAC3, depending on sequence similarity and domain organization. Histone acetylation plays an important role in regulation of gene expression. In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation [4]. May be identical to EC 3.5.1.17, acyl-lysine deacylase.
CAS REGISTRY NUMBER
COMMENTARY hide
9076-57-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Fluor de Lys + H2O
?
show the reaction diagram
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-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-[(9H-fluoren-3-ylmethyl)(3-phenoxybenzyl)amino]-N-hydroxyhexanamide
simultaneous and efficient interactions of compound with both the enzyme surface and the tubular binding pocket, through proper selection of its arm groups, are critical for potential antagonist activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O67135_AQUAE
Aquifex aeolicus (strain VF5)
375
0
42663
TrEMBL
Mitochondrion (Reliability: 3)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling studies using inhibitor 6-[(9H-fluoren-3-ylmethyl)(3-phenoxybenzyl)amino]-N-hydroxyhexanamide and histone deacetylase-like protein, PDB ID: 1C3R. Inhibitor fills the equivalent space at the protein surface and occupies the catalytic binding site, coordinating the fundamental zinc ion
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Terracciano, S.; Chini, M.G.; Riccio, R.; Bruno, I.; Bifulco, G.
Design, synthesis, and biological activity of hydroxamic tertiary amines as histone deacetylase inhibitors
ChemMedChem
7
694-702
2012
Homo sapiens, Aquifex aeolicus (O67135)
Manually annotated by BRENDA team