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. 2001 Nov 2;288(3):666-9.
doi: 10.1006/bbrc.2001.5824.

The catalytic properties of human carbonic anhydrase IX

T Wingo  1 , C Tu, P J Laipis, D N Silverman
Affiliations

The catalytic properties of human carbonic anhydrase IX

T Wingo et al. Biochem Biophys Res Commun. .

Abstract

Human carbonic anhydrase IX (CA IX) is an integral membrane protein and a member of the alpha class of carbonic anhydrases that includes the human and animal enzymes. We have prepared a truncated, recombinant form of human CA IX of 255 residues consistent with full-length human CA II, among the most efficient of the carbonic anhydrases. Catalysis by and inhibition of this form of human CA IX has been investigated using stopped-flow spectrophotometry and 18O exchange measured by mass spectrometry. In kinetic constants for the hydration of CO2, CA IX closely resembled CA II with maximal proton transfer-dependent 18O exchange near 1 micros(-1) and kcat/Km near 55 microM(-1) x s(-1). Human CA IX was very strongly inhibited by three classic sulfonamides and cyanate, with inhibition constants that are close to those for CA II.

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