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. Author manuscript; available in PMC: 2016 Jan 1.
Published in final edited form as: Crit Rev Biochem Mol Biol. 2014 Nov 3;50(1):31–53. doi: 10.3109/10409238.2014.978975

Table 2.

Summary of Rtt109 kinetic parameters.

Enzyme form Protein substrate Protein KM (μM) kcat (s−1) acetyl-CoA KM (μM) Technical notes Reference
Rtt109 H31–20 83 ± 29 0.0017 ± 0.0001 0.3 ± 0.1 acetyl-CoA + protein substrate pairing unclear (Berndsen et al., 2008)
H3 8.1 ± 0.1 0.0033 ± 0.0003 0.3 ± 0.1 acetyl-CoA + protein substrate pairing unclear (Berndsen et al., 2008)
H3–H4 2.9 ± 0.6 0.0044 ± 0.0009 0.3 ± 0.1 acetyl-CoA + protein substrate pairing unclear (Berndsen et al., 2008)
Rtt109-Vps75 H31–20 75 ± 15 0.13 ± 0.04 1.0 ± 0.2 acetyl-CoA + protein substrate pairing unclear (Berndsen et al., 2008)
H31–20 112 ± 11   0.11 ± 0.01 0.3 ± 0.1 – (Albaugh et al., 2010)
H3 5.8 ± 0.8 0.21 ± 0.04 1.0 ± 0.2 acetyl-CoA + protein substrate pairing unclear (Berndsen et al., 2008)
H3 – 0.19 ± 0.01 1.0 ± 0.2 – (Tsubota et al., 2007)
H3 3.9 ± 2   0.069 ± 0.001 NR 0.2 eq. Vps75 (Kolonko et al., 2010)
H3 6.5 ± 2   0.62 ± 0.02 NR 8 eq. Vps75 (Kolonko et al., 2010)
H3 7 ± 1 0.63 ± 0.02 NR – (Albaugh et al., 2010)
H3 8.5 ± 0.7 0.375 ± 0.027 8.0 ± 2.0 – (Tang et al., 2008)
H3–H4 1.4 ± 0.4 0.11 ± 0.05 1.0 ± 0.2 acetyl-CoA-protein substrate pairing unclear (Berndsen et al., 2008)
H3–H4 2.12 ± 0.63 0.068 ± 0.004 NR 6 eq. Vps75 (Tsubota et al., 2007)
H3–H4 0.84 ± 0.28 0.34 ± 0.04 NR – (Tang et al., 2011)
H3–H4 0.5 ± 0.3 0.041 ± 0.004 NR 0.2 eq. Vps75 (Kolonko et al., 2010)
H3–H4 0.1 ± 0.1   0.13 ± 0.007 NR 8 eq. Vps75 (Kolonko et al., 2010)
yH3–H4 1.4 ± 0.4 0.41 ± 0.05 NR Tetramer (Kolonko et al., 2010)
yH3(A110E)–H4 2.4 ± 0.7 0.39 ± 0.06 NR Dimeric form (Kolonko et al., 2010)
Rtt109-Asf1 H3–H4 1.19 ± 0.34 0.021 ± 0.002 Low micromolar – (Tsubota et al., 2007)
H3–H4 1.84 ± 0.81 0.015 ± 0.002 NR – (Tang et al., 2011)

In general, the KM for protein substrate decreases from the peptide to the full-length H3 to the H3–H4 tetramer form, with or without Vps75 present. In general, the addition of Vps75 leads to an increase in kcat regardless of protein substrate, while the KM for acetyl-CoA is relatively constant. NR, no report.