Literature summary 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.

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.5.1.98	Homo sapiens	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.5.1.98	N6-lysine acetylated histone H2A + H2O	substrate of isoforms HDAC1, HDAC2, HDAC. Isoform HDAC3 preferentially cleeaves lysines 5 H2A	Homo sapiens	histone H2A + acetate	-	?
3.5.1.98	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

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

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
3.5.1.98	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)