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3.5.1.98: histone deacetylase

This is an abbreviated version!
For detailed information about histone deacetylase, go to the full flat file.

Word Map on EC 3.5.1.98

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hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone =

Synonyms

acetyl-lysine deacetylase, AhHDA1, AtHD1, class I acetyl-lysine deacetylase, class I HDAC, class I histone deacetylase, class II Hda1 HDAC, class II histone deacetylase, class IIa HDAC, class IIa histone deacetylase, Clr6, cytoplasmic deacetylase, deacetylase-like amidohydrolase, dRPD3, FB188 HDAH, Glyma.01 g245100, Glyma.04 g000200, Glyma.04 g187000, Glyma.04 g187100, Glyma.05 g012900, Glyma.05 g021400, Glyma.05 g040600, Glyma.05 g192600, Glyma.06 g000100, Glyma.06 g178700, Glyma.11 g000300, Glyma.11 g187800, Glyma.12 g086700, Glyma.12 g188200, Glyma.17 g078000, Glyma.17 g085700, Glyma.17 g120900, Glyma.17 g229600, GmHDA1, GmHDA10, GmHDA11, GmHDA12, GmHDA13, GmHDA14, GmHDA15, GmHDA16, GmHDA17, GmHDA18, GmHDA2, GmHDA3, GmHDA4, GmHDA5, GmHDA6, GmHDA7, GmHDA8, GmHDA9, GmHDAC, HD1B, HD2, HD8, HDA, HDA-1, HDA-2, HDA-3, HDA-4, hda1, HDA15, HDA19, HDA9, HdaA, HDAC, HDAC 11, HDAC 3, HDAC1, HDAC10, HDAC2, HDAC2-1, HDAC2-2, HDAC3, HDAC4, HDAC5, HDAC6, HDAC6p114, HDAC6p131, HDAC7, HDAC8, HDAC9, HDAH, HDLP, HDT1, HDT2, histone deacetylase, histone deacetylase 1, histone deacetylase 10, histone deacetylase 11, histone deacetylase 2, histone deacetylase 3, histone deacetylase 4, histone deacetylase 6, histone deacetylase 7, histone deacetylase 8, histone deacetylase-1, histone deacetylase-7, histone deacetylase-like amidohydrolase, histone deacetylase-like protein, histone deacetylase1, Hos2, HosB, PA3774, pfHDAC-1, RPD3, Set3 complex, Set3C, tubulin deacetylase, zinc-dependent histone deacetylase, Zn(II)-dependent deacetylase, Zn-HDAC

ECTree

     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

Metals Ions

Metals Ions on EC 3.5.1.98 - histone deacetylase

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
Zn2+, Mg2+, or Mn2+ is required. Zn2+ is the most efficient
Na+
-
Na+ binds more weakly to both monovalent cation sites and activates HDAC8 to a lesser extent than K+
Ni2+
ratio of kcat to KM value in presence of metal ion in decreasing order: Co(II), Fe(II), Zn(II), Ni(II)
Zinc
-
enzyme active site consists of a tubular pocket, a zinc-binding site and two D-H charge-relay systems
additional information