2HKK

Carbonic anhydrase activators: Solution and X-ray crystallography for the interaction of andrenaline with various carbonic anhydrase isoforms

Summary for 2HKK

• Entry DOI: 10.2210/pdb2hkk/pdb
• Descriptor: Carbonic anhydrase 2, ZINC ION, MERCURY (II) ION, ... (5 entities in total)
• Functional Keywords: carbonic anhydrase, activators, lyase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P00918
• Total number of polymer chains: 1
• Total formula weight: 29738.27

Authors

Temperini, C.,Innocenti, A.,Vullo, D.,Scozzafava, A.,Supuran, C.T. (deposition date: 2006-07-05, release date: 2007-05-22, Last modification date: 2023-08-30)

Primary citation

Temperini, C.,Innocenti, A.,Scozzafava, A.,Mastrolorenzo, A.,Supuran, C.T.
Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV.
Bioorg.Med.Chem.Lett., 17:628-635, 2007

PubMed Abstract: The activation of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1) with L-adrenaline and histamine has been investigated by kinetic and X-ray crystallographic studies. L-Adrenaline behaves as a potent activator of isozyme CA I (activation constant of 90 nM), being a much weaker activator of isozyme CA II (activation constant of 96 microM). Isoforms CA IV, VA, VII, and XIV were activated by L-adrenaline with K(A)s in the range of 36-63 microM. The X-ray crystal structure of the CA II-L-adrenaline adduct revealed that the activator plugs the entrance of the active site cavity, obstructing it almost completely.

PubMed: 17127057
DOI: 10.1016/j.bmcl.2006.11.027

Experimental method

X-RAY DIFFRACTION (1.9 Å)