Title : Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II.

Pub. Date : 1993 Dec 25

PMID : 8262987






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The side chain hydroxyl group causes: stabilization of zinc-hydroxide relative to zinc-water (pKa increases approximately 2 units); stabilization of the transition state for bicarbonate dehydration relative to the CAII.HCO3- complex (approximately 5 kcal/mol); and destabilization of the CAII.HCO3- complex (approximately 0.8 kcal/mol). Bicarbonates carbonic anhydrase 2 Homo sapiens
2 The side chain hydroxyl group causes: stabilization of zinc-hydroxide relative to zinc-water (pKa increases approximately 2 units); stabilization of the transition state for bicarbonate dehydration relative to the CAII.HCO3- complex (approximately 5 kcal/mol); and destabilization of the CAII.HCO3- complex (approximately 0.8 kcal/mol). Bicarbonates carbonic anhydrase 2 Homo sapiens
3 The side chain hydroxyl group causes: stabilization of zinc-hydroxide relative to zinc-water (pKa increases approximately 2 units); stabilization of the transition state for bicarbonate dehydration relative to the CAII.HCO3- complex (approximately 5 kcal/mol); and destabilization of the CAII.HCO3- complex (approximately 0.8 kcal/mol). Bicarbonates carbonic anhydrase 2 Homo sapiens
4 These data are consistent with the hydroxyl group of Thr199 forming a hydrogen bond with the transition state and a non-hydrogen-bonded van der Waals contact with CAII.HCO3-. Bicarbonates carbonic anhydrase 2 Homo sapiens