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. Author manuscript; available in PMC: 2009 Aug 8.
Published in final edited form as: Curr Opin Struct Biol. 2008 Dec;18(6):682–689. doi: 10.1016/j.sbi.2008.11.004

Table 2.

Comparison of kinetic constants for HAT catalyzed acetyl transfer

HAT kcat, s−1 Km AcCoA, µM Km peptide, µM Reference
p300 4.1 ± 0.1 × 100 40 ± 0.6 1.6 ± 0.1 × 102a [26•]
Gcn5 1.7 ± 0.1 × 100 2.5 ± 1.4 4.9 ± 0.8 × 102 b [18]
Rtt109 1.7 ± 0.1 × 10−3 0.3 ± 0.1 8.3 ± 2.9 × 101 c [29•]
Rtt109•Vps75 1.3 ± 0.4 × 10−1 1.0 ± 0.2 7.5 ± 1.5 × 101 c [29•]
Esa1 1.9 ± 1.0 × 10−3 1.0 ± 0.4 1.4 ± 1.0 × 103 d [40]; C.E.B. and
J.M.D.,
unpublished data
Piccolo NuA4 1.6 ± 0.1 × 100 2.5 ± 0.3 2.2 ± 0.3 × 102 d [23•]
a

Calculated using a peptide of H4 residues 4 to 15

b

Calculated using a peptide of H3 residues 1 to 20 plus a C-terminal cysteine

c

Calculated using a peptide of H3 residues 1 to 20

d

Calculated using a peptide of H4 residues 1 to 20