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Information on EC 3.5.1.98 - histone deacetylase and Organism(s) Gallus gallus and UniProt Accession P56517

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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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Gallus gallus
UNIPROT: P56517
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Word Map
The taxonomic range for the selected organisms is: Gallus gallus
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
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N6-lysine acetylated histone H2A-H2B dimer + H2O
histone H3-H4 dimer + acetate
show the reaction diagram
-
-
-
?
N6-lysine acetylated histone H3-H4 tetramer + H2O
histone H3-H4 tetramer + acetate
show the reaction diagram
preferred substrate
-
-
?
N6-lysine acetylated histone H2A-H2B dimer + H2O
histone H3-H4 dimer + acetate
show the reaction diagram
-
isoform HD2, slightly preferred substrate
-
-
?
N6-lysine acetylated histone H3-H4 tetramer + H2O
histone H3-H4 tetramer + acetate
show the reaction diagram
-
isoform HD1, preferred substrate
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
10 mM, 66% inhibition
NaCl
inhibitory in sodium phosphate/citric acid buffer, 50% inhibition at 100 mM
Butyrate
-
non-competitive
additional information
-
in phosphate buffer, the presence of NaCl is inhibitory
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
in Tris/HCl buffer, optimum concentration of NaCl is 50 mM for isoforms HD1 and HD2 and 100 mM for the nuclear matrix form
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021 - 0.08
Butyrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
-
isoform HD2
7 - 7.5
-
nuclear matrix form of enzyme
7.5
-
isoform HD1
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
calculated
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform HDAC1
Swissprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
associated to
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HDAC1_CHICK
480
0
54939
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54938
1 * 66000, SDS-PAGE, 1 * 54938, calculated
66000
1 * 66000, SDS-PAGE, 1 * 54938, calculated
72000
gel filtration
220000
-
isoform HD2, gel filtration
400000
-
enzyme complex solubilized from nuclear matrix, gel filtration
55000
-
isoform HD1, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 66000, SDS-PAGE, 1 * 54938, calculated
additional information
-
isoform HD2 dissociates into HD1 when treated with 1.6 M NaCl or applied to a Q-Sepharose column. The active form of enzyme is a high-molecular-mass complex associated with proteins that are components of the nuclear matrix
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, W.; Chen, H.Y.; Davie, J.R.
Properties of chicken erythrocyte histone deacetylase associated with the nuclear matrix
Biochem. J.
314
631-637
1996
Gallus gallus
-
Manually annotated by BRENDA team
Sun, J.M.; Chen, H.Y.; Moniwa, M.; Samuel, S.; Davie, J.R.
Purification and characterization of chicken erythrocyte histone deacetylase 1
Biochemistry
38
5939-5947
1999
Gallus gallus (P56517), Gallus gallus
Manually annotated by BRENDA team