Activation of carbonic anhydrase II by active-site incorporation of histidine analogs.

doi:10.1016/j.abb.2003.11.006

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Article

Activation of carbonic anhydrase II by active-site incorporation of histidine analogs.

Archives of biochemistry and biophysics - 15 Jan 2004

Elder Ileana, Han Shoufa, Tu Chingkuang, Steele Heather, Laipis Philip J, Viola Ronald E, Silverman David N

Abstract excerpt

The hydration of CO2 catalyzed by human carbonic anhydrase II (HCA II) is accompanied by proton transfer from the zinc-bound water of the enzyme to solution. We have replaced the proton shuttling residue His 64 with Ala and placed cysteine residues within the active-site cavity by mutating sites Trp 5, Asn 62, Ile 91, and Phe 131. These mutants were modified at the single inserted cysteine with imidazole analogs...

Topics

Binding Sites
Carbon Dioxide
Carbonic Anhydrase II
Histidine
Humans
Hydrogen-Ion Concentration
Kinetics
Mutation
Protein Structure, Tertiary
Protons

Source

Open in PubMed

Identifiers

PMID: 14984209
DOI: 10.1016/j.abb.2003.11.006

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