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. 2002 Nov;13(11):3878–3889. doi: 10.1091/mbc.E02-05-0302

Table 2.

Properties of six Dictyostelium PDEs

Phosphodiesterase PDE1 PDE2 PDE3 PDE4* PDE5 PDE6
Name of gene psdA regA DdPDE3 DdPDE4 gbpA gbpB
Localization Cell surface Cytosol Cytosol Cell surface Cytosol Cytosol
Class II I I I II II
cAMP/cGMP selectivity 3 >200 ∼0.0015 Unknown <0.003 9
cAMP hydrolysis
KM (μM) 0.8 5 >100 Unknown >500 200
(150) (1800)
VMAX (pmol/min/mg) 700 50 Unknown 5200
KA (μM) Unknown >300 0.7
AMAX 1.47
cGMP hydrolysis
KM (μM) 1.8 >1000 0.22 * 5.2–20 800
VMAX (pmol/min/mg) 490 2 * 390 2400
KA (μM) * 0.16 2.3
AMAX 2.40 1.86
Intracellular cAMP degradation (pmol/min/mg)
 0.1 μM 1 * 2.6
 1 μM 8 * 26
 5 μM 25 * 127
Intracellular cGMP degradation (pmol/min/mg)
 0.1 μM 0.6 * 3.3 0.3
 1 μM 1.6 * 48 3.0
 5 μM 1.9 * 163 15

PDE4 

*

, the enzyme has not been characterized biochemically; sequence data suggest that the enzyme is cAMP specific and has a signal sequence and two transmembrane segments predicting the catalytic domain to be extracellular. The cAMP/cGMP selectivity refers to the calculated VMAX/KM for cAMP divided by the VMAX/KM for cGMP. The data for the KM in parentheses refer to the cAMP concentration inducing half-maximal inhibition of the hydrolysis of cGMP. The kinetic constants were derived from Van Haastert et al. (1983) for PDE1; from Shaulsky et al. (1998) and Thomason et al. (1998) for PDE2, and from Figure 4 to calculate the VMAX in vivo, assuming that cAMP hydrolysis in gbpA/gbpB is derived from RegA; for PDE6 from Kuwayama et al. (2001) for PDE3; from Figure 7 for PDE5; and from Figure 6 for PDE6. The rates of intracellular degradation were calculated using the obtained kinetic constants and are presented for three concentrations representing basal levels (0.1 μM), maximal levels in wild-type cells (1 μM), and maximal levels in some deletion mutants (5 μM).