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. Author manuscript; available in PMC: 2009 Dec 26.
Published in final edited form as: Chem Biol. 2009 Jun 26;16(6):605–612. doi: 10.1016/j.chembiol.2009.05.007

Table 1.

Steady-state kinetic parameters for ClpXP degradation of peptide substrates.

name Vmax min−1 ClpP−1 KM µM Vmax with SspB min−1 ClpP−1 cost ATP/peptide with SspB Sequence length
[G7] 13.7 ± 1.3 5.4 ± 1.9 13.5 ± 0.7 30 ABZ-FAPHMALVPYNO2G7KKAANDENYALAA 30
[G10] 14.3 ± 0.8 6.1 ± 0.2 11.5 ± 0.4 30 ABZ-FAPHMALVPYNO2G10KKAANDENYALAA 33
[G5KKG5] 14.5 ± 1.9 4.5 ± 2.2 12.1 ± 0.1 36 ABZ-FAPHMALVPYNO2G5KKG5AANDENYALAA 33
[β]10 9.8 ± 0.9 4.1 ± 0.3 8.8 ± 1.1 43 ABZ-FAPHMALVPYNO2β10KKAANDENYALAA ABZ- 33
[γ]10 6.4 ± 0.3 3.7 ± 0.6 6.5 ± 0.4 57 FAPHMALVPYNO2γ10KKAANDENYALAA ABZ- 33
[ε]10 6.1 ± 0.6 4.7 ± 0.4 5.9 ± 0.3 61 FAPHMALVPYNO2ε10KKAANDENYALAA 33
[O]5 7.0 ± 0.2 4.3 ± 0.4 6.8 ± 1.3 53 ABZ-FAPHMALVPYNO2O5KKAANDENYALAA ABZ- 33
[U]4 6.2 ± 0.6 9.0 ± 2.0 7.8 ± 0.5 47 FAPHMALVPYNO2U4KKAANDENYALAA 27
[P5] 11.4 ± 0.2 n.d. 12.9 ± 1.1 45 ABZ-FAPHMALVPYNO2P5KKAANDENYALAA ABZ- 28
[P10] 6.4 ± 0.2 2.8 ± 0.2 6.5 ± 0.2 65 FAPHMALVPYNO2P10KKAANDENYALAA ABZ- 33
[P15] 3.4 ± 0.8 3.6 ± 0.7 3.3 ± 0.3 125 FAPHMALVPYNO2P15KKAANDENYALAA 38
[VG]5 14.4 ± 1.7 3.4 ± 0.3 13.6 ± 0.4 30 ABZFAPHMALVPYNO2 [VG]5KKAANDENYALAA 33
[DVG]5 14.0 ± 0.4 6.7 ± 1.6 14.2 ± 0.2 28 ABZ-FAPHMALVPYNO2[dVG]5KKAANDENYALAA 33
[FG]5 12.1 ± 1.7 4.2 ± 1.0 14.1 ± 0.8 22 ABZ-FAPHMALVPY [FG]5KKAANDENYALAA 33
[Q10] 8.7 ± 0.5 9.1 ± 1.7 8.8 ± 0.8 48 ABZ-FAPHMALVPYNO2Q10KKAANDENYALAA ABZ- 33
[E10] 6.0 ± 0.1 2.0 ± 0.1 6.3 ± 0.2 62 FAPHMALVPYNO2E10KKAANDENYALAA ABZ- 33
[K10] 2.7 ± 0.1 • 0.2 2.8 ± 0.1 160 FAPHMALVPYNO2K10KKAANDENYALAA ABZ- 33
[R10] 8.0 ± 0.4 0.2 ± 0.1 8.4 ± 0.1 53 FAPHMALVPYNO2R10KKAANDENYALAA 33

β (β-alanine); γ (γ-aminobutyric acid), ε (ε-amino caproic acid); O (8-aminooctanoic acid), U (11-aminoundecanoic acid).

Vmax and KM values are means of 2–3 independent determinations (n) with errors calculated as 1(n1)1n(valuemean)2.