. 1999 Oct;65(10):4559–4567. doi: 10.1128/aem.65.10.4559-4567.1999

TABLE 3.

Kinetic parameters for T. maritima I-1-Pase hydrolysis of inositol phosphate substrates

Substrate	K_m (mM)	V_max (μmol of P_i min⁻¹ mg of protein⁻¹)
Substrate	K_m (mM)	Partially purified enzyme	Recombinant enzyme
dl-I-1-P	0.145 ± 0.016^a	21.3 ± 0.6^a
d-I-1-P	0.148 ± 0.013^a	44.6 ± 1.1^a
	0.126 ± 0.010^b		443 ± 10^b
l-I-1-P			23^c
I-2-P	0.460 ± 0.05^a	5.8 ± 0.3^a

The K_m and V_max values were determined with partially purified I-1-Pase (although the same relative specificities were observed with the recombinant enzyme).

Determined with homogeneous recombinant enzyme.

Estimated from the relative rates of the recombinant enzyme with pure d-I-1-P and with l-I-1-P.