Simple methanesulfonates are hydrolyzed by the sulfatase carbonic anhydrase activity

Figures & data

Scheme 1.  Reactions (1–10) catalyzed by α-CAs.

Scheme 2.  Reactions 11 and 12 catalyzed by α-CAs: 4-nitrophenyl acetate/phosphate hydrolysis¹⁸.

Table 1.  Inhibition data (K_I values, μM) against hCA I, hCA II, hCA IV and hCA VI of compounds 4–16 and standard sulfonamide inhibitors (EZA, ZNS and AZA) by an esterase method with 4-nitrophenyl acetate as substrate.

Inhibitor	hCA I	hCA II	hCA IV	hCA VI
4	27.36	8.70	15.43	105.2
5	48.54	12.24	26.48	162.1
6	22.14	4.23	9.12	28.43
7	10.24	5.6	9.7	210
8	19.54	7.41	12.34	85.04
9	10.8	0.10	10.8	524
11	478.3	35.42	45.06	458.1
13	196.2	28.51	41.64	312.7
15	79.13	6.45	8.14	12.1
10	7.35	0.52	0.49	6.83
12	4012	9.92	10.94	608
14	55.7	1.32	1.84	3.27
16	60.23	2.98	3.56	217
EZA	3.75	0.32	0.84	1.58
ZNA	14.8	1.07	38.45	2.42
AZA	36.2	0.37	0.578	0.34

Mean from at least three determinations. Errors were in the range of ± 3% of the reported value (data not shown).

AZA, acetazolamide; EZA, sulfonamides ethoxzolamide; hCA, human erythrocyte carbonic anhydrase; ZNA, zonisamide.

Figure 1.  Structure of tested compounds 10–16 and some medical used sulfonamides.

Scheme 3.  The hydrolysis reaction of compound 4, 5 and 6 with CA II isoenzyme.

Innocenti A, Supuran CT. Paraoxon, 4-nitrophenyl phosphate and acetate are substrates of a- but not of β-, γ- and ζ-carbonic anhydrases. Bioorg Med Chem Lett 2010;20:6208–6212.

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