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Article

Catalysis by mutants of human carbonic anhydrase II: effects of replacing hydrophobic residues 198 and 204.

Biochimica et biophysica acta - 20 Oct 1992

Taoka S, Chen X, Tarnuzzer R W, Van Heeke G, Tu C, Silverman D N

Abstract excerpt

Previous studies shows that the replacement of Phe-198 in carbonic anhydrase III to the corresponding Leu residue found in carbonic anhydrase II caused the appearance of isozyme II-like activity (LoGrasso et al. (1991) Biochemistry 30, 8463-8470). Carbonic anhydrase II is more efficient in the catalysis of CO2 hydration by 500-fold and has an apparent pKa for this catalysis about two pKa units above that of...

Topics

Base Sequence
Bicarbonates
Biological Transport
Carbon Dioxide
Carbonic Anhydrases
Catalysis
Humans
Molecular Sequence Data
Mutation
Protons
Structure-Activity Relationship

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Identifiers

PMID: 1327160
DOI: 10.1016/0167-4838(92)90056-j

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1327160-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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