Literature summary for 3.5.1.98 extracted from

Johnson, C.A.; White, D.A.; Lavender, J.S.; O'Neill, L.P.; Turner, B.M.
Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70 (2002), J. Biol. Chem., 277, 9590-9597.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N6-lysine acetylated histone H2A + H2O	substrate of isoforms HDAC1, HDAC2, HDAC. Isoform HDAC3 preferentially cleeaves lysines 5 H2A	Homo sapiens	histone H2A + acetate	-	?
N6-lysine acetylated histone H4 + H2O	substrate of isoforms HDAC1, HDAC2, HDAC. HDAC3 preferentially cleeaves lysines 5 and 12 of H4. H4 tails in purified mononucleosomes are deacetylated by isoforms HDAC1 and HDAC3 only in presence of ATP	Homo sapiens	histone H4 + acetate	-	?

Subunits

Subunits	Comment	Organism
More	isoforms HDAC1, HDAC2, HDAC3 co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	required for deacetylation of histone H4 in purified nucleosomes by isoforms HDAC1 and HDAC3. ATP also enhances cleavage of free, non-nucleosomal histones by HDAC1 and HDAC3	Homo sapiens

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Release 2023.1 (January 2023)