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Information on EC 3.5.1.98 - histone deacetylase and Organism(s) Alcaligenes sp. and UniProt Accession Q70I53

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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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Alcaligenes sp.
UNIPROT: Q70I53
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Word Map
The taxonomic range for the selected organisms is: Alcaligenes sp.
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
deacetylase-like amidohydrolase
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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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2,3,3,4,4,5,5,6,6,7,7-dodecafluorooctanedioic acid hydroxyamide phenylamide
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N-hydroxy-4-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}butanamide
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N-hydroxy-5-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}pentanamide
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N-hydroxy-6-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}hexanamide
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N-hydroxy-7-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}heptanamide
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N-hydroxy-8-{[5-(propan-2-yl)naphthalene-1-sulfonyl]amino}octanamide
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N-hydroxy-N~3~-[5-(propan-2-yl)naphthalene-1-sulfonyl]-beta-alaninamide
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suberoylanilide hydroxamic acid
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suberoylanilide trifluoromethylketone
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trichostatin A
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additional information
enzyme binding mechanisms, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
enzyme kinetic calculations, overview
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
inhibition kinetic calculations, Kd values, detailed overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Bordetella sp. strain FB188
SwissProt
Manually annotated by BRENDA team
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Meyners, C.; Baud, M.G.; Fuchter, M.J.; Meyer-Almes, F.J.
Kinetic method for the large-scale analysis of the binding mechanism of histone deacetylase inhibitors
Anal. Biochem.
460
39-46
2014
Homo sapiens (Q13547), Homo sapiens (Q9BY41), Homo sapiens (Q9UBN7), Homo sapiens, Alcaligenes sp. (Q70I53), Alcaligenes sp. DSM 11172 (Q70I53)
Manually annotated by BRENDA team