Sulphonamide inhibition studies of the β-carbonic anhydrase from the bacterial pathogen Clostridium perfringens

Figures & data

Table 1. Inhibition of human isoforms hCA I and hCA II (off-target enzymes), as well as the bacterial enzyme from C. perfringens (CpeCA) with sulphonamides 1–24 and the clinically used drugs AAZ–HCT, by a stopped-flow, CO₂ hydrase assay [52].

	KI* (nM)
Inhibitor/Enzyme class	hCA I^aα	hCA II^aα	CpeCA^bβ
1	28,000	300	451
2	25,000	240	402
3	79	8	210
4	78,500	320	379
5	25,000	170	3690
6	21,000	160	2430
7	8300	60	443
8	9800	110	320
9	6500	40	713
10	7300	54	4670
11	5800	63	8755
12	8400	75	7635
13	8600	60	297
14	9300	19	460
15	5500	80	131
16	9500	94	145
17	21,000	125	314
18	164	46	1268
19	109	33	179
20	6	2	105
21	69	11	697
22	164	46	513
23	109	33	312
24	95	30	51.2
AAZ	250	12	49.1
MZA	50	14	113
EZA	25	8	71.6
DCP	1200	38	68.0
DZA	50,000	9	37.4
BRZ	45,000	3	121
BZA	15	9	497
TPM	250	10	204
ZNS	56	35	>100,000
SLP	1200	40	389
IND	31	15	173
VLX	54,000	43	160
CLX	50,000	21	312
SLT	374	9	63.1
SAC	18,540	5959	>100,000
HCT	328	290	219

* Errors in the range of 5–10% of the shown data, from three different assays.

^a Human recombinant isozymes, stopped flow CO₂ hydrase assay method, from reference [3–5].

^b Recombinant bacterial enzyme, stopped flow CO₂ hydrase assay method, this work.

Khalifah RG. The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C. J Biol Chem 1971;246:2561–73.

 PubMed Web of Science ®Google Scholar