Metal Ion Dependent Binding of Sulphonamide to Carbonic Anhydrase

Je, Coleman

doi:10.1038/214193a0

Cited by 119 publications

(33 citation statements)

References 5 publications

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“…One is metal complex forming anions and others are sulfonamides and their isosteres. 125,126 Structural data show that the inhibitors ionize upon binding with the enzyme to yield an NH À group that relocates the zinc hydroxide ion and shares a hydrogen bond with Thr199. 64 Approximately 25 clinically used drugs have been developed against CAs that used as diuretics, antiglaucoma drugs, anticonvulsants and anticancer agents.…”

Section: Inhibitors Of Carbonic Anhydrasementioning

confidence: 98%

Structure, function and applications of carbonic anhydrase isozymes

Hassan

Shajee

Waheed

et al. 2013

Bioorganic & Medicinal Chemistry

224

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Section: Inhibitors Of Carbonic Anhydrasementioning

confidence: 98%

Structure, function and applications of carbonic anhydrase isozymes

Hassan

Shajee

Waheed

et al. 2013

Bioorganic & Medicinal Chemistry

224

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“…Cobalt(II) carbonic anhydrase has 50% of the carbon dioxide hydration activity of the native zinc enzyme. In contrast, the activities of the cupric, ferrous, nickel(II) and manganese(II) derivatives are negligible (Coleman, 1967;Lindskog & Nyman, 1964;Thorslund & Lindskog, 1967), despite the similarity of these metal ions to zinc in terms of charge, size and pK. The three-dimensional structure of human carbonic anhydrase II is known at high resolution (Liljas, Kannan, Bergst6n, Waara, Fridborg, Strandberg, Carlbom, JS_rup, l_,6vgren & Petef, 1972;H~kansson, Carlsson, Svensson & Liljas, 1992).…”

Section: Introductionmentioning

confidence: 95%

X-ray analysis of metal-substituted human carbonic anhydrase II derivatives

Håkansson¹,

Wehnert²,

Liljas³

1994

Acta Cryst D

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Metal-substituted crystals of human carbonic anhydrase II belonging to space group P2[1 with cell dimensions a = 42.7, b = 41.7, c = 73.0A and /3 = 104.6 ° were analyzed crystallographically. The resolution limit ranged from 1.82 to 1.92A with high completeness (86.2-90.7%). Cobalt(II)-substituted carbonic anhydrase has a tetrahedral coordination around the metal both at pH 6 and pH 7.8, similar to the native zinc enzyme. In contrast, the catalytically inactive copper(II), nickel(II) and manganese(II) derivatives showed increased coordination number around the metal ion. Whereas the copper is best described as penta-coordinated, the nickel and manganese are best described as hexa-coordinated. The results are briefly compared with spectroscopic observations and our current view on carbonic anhydrase catalysis.

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“…Carbonic anhydrase has a narrow range of metals that yield an active enzyme (Lindskog and Nyman, 1964;Thorslund and Lindskog, 1967;Coleman, 1967). The zinc can be replaced only with cobalt(I1) and still maintain significant activity.…”

Section: Metal Coordination In Carbonic Anhydrasementioning

confidence: 99%