Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I.

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Citation

Temperini C, Scozzafava A, Supuran CT

Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I.

Bioorg Med Chem Lett. 2006 Oct 1;16(19):5152-6. Epub 2006 Jul 25.

PubMed ID
16870440 [ View in PubMed
]
Abstract

The X-ray crystallographic structure for the adduct of an activator with human carbonic anhydrase isozyme I (hCA I) is reported. L-Histidine binds deep within the enzyme active site, participating in a network of hydrogen bonds involving its carboxylate moiety and the zinc-bound water molecule, as well as the imidazole of His200, being in van der Waals contacts with Thr199, His200, His64, and His67. This binding is very different from that to the other major cytosolic isozyme hCA II.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Carbonic anhydrase 1P00915Details