Table 2.

Additional phosphatase constants.

DOI: http://dx.doi.org/10.7554/eLife.24665.010

Phosphatase	Substrate	Constant	Value	Source figure or (reference)
MLCP		Σphys*	~15	Figure 8—figure supplement 2
	pMyBP	Km	~1.7 μM	Figure 2—figure supplement 1
		kcat	~0.18 s−1	Figure 2—figure supplement 1
	pC-ERMAD	Km	>2.5 μM	Figure 2—figure supplement 1
		kcat /Km	2.6 ± 0.03 × 10−4 nM−1 s−1	Figure 2—figure supplement 1
	pMRLC	Km	~16 μM	(Kawano et al., 1999)

Phosphatase	Substrate	Constant	Value	Source figure or (reference)
PPU		Σphys*	~24	Figure 8—figure supplement 2
	pCPI-17	Km	15 ± 2 μM	Figure 7—figure supplement 2
		Km(0°C)	14 ± 3 μM	Figure 7—figure supplement 2

Phosphatase	Substrate	Constant	Value	Source figure or (reference)
PPUa	pCPI-17	kcat (30°C)/kcat (0°C)	8.3 ± 0.8	Figure 7—figure supplement 1
		kcat [PPU]a/M/Km	0.024 ± 0.001 s−1 ml mg−1	Figure 7 and Figure 7—figure supplement 1
		[PPU]a/M	8.9 ± 0.9 pmol/mg	Figure 8

Phosphatase	Substrate	Constant	Value	Source figure or (reference)
PPUb	pCPI-17	kcat [PPU]b/M/Km	0.0045 ± 0.0002 s−1 ml mg−1	Figure 7 and Figure 7—figure supplement 1

All parameters are at 30°C except as specified.

phys: Physiological total (bound plus unbound) concentration; these values are computed using an estimated physiological total protein concentration of 170 mg/ml (Wiśniewski et al., 2014).

M: total extract protein concentration.

Σ: Competition factor from other substrates (see Supplementary file 1).