Table 1.
Isozyme | kcat (s−1) a | KM (mM) a | (kcat)L-Trp (s−1) b | KA (μM) L-Trp c |
---|---|---|---|---|
hCA I d | 2.0 × 105 | 4.0 | 3.4 × 105 | 44 |
hCA II d | 1.4 × 106 | 9.3 | 4.9 × 106 | 27 |
BsuCA 1 e | 6.4 × 105 | 16.4 | 25.9 × 105 | 1.25 |
FtuCA e | 9.8 × 105 | 11.0 | 15.7 × 105 | 34.1 |
Observed catalytic rate without activator. K M values in the presence and the absence of activators were the same for the various CAs (data not shown).
Observed catalytic rate in the presence of 10 μM activator.
The activation constant (K A) for each enzyme was obtained by fitting the observed catalytic enhancements as a function of the activator concentration 21–29 . Mean from at least three determinations by a stopped-flow, CO2 hydrase method 20 . Standard errors were in the range of 5–10% of the reported values (data not shown).
Human recombinant isozymes, from Supuran 8 a.
Bacterial recombinant enzyme, this work.