Proposal for a hydrogen bond network in the active site of the prototypic gamma-class carbonic anhydrase.

doi:10.1021/bi052507y

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Proposal for a hydrogen bond network in the active site of the prototypic gamma-class carbonic anhydrase.

Biochemistry - 25 Apr 2006

Zimmerman Sabrina A, Ferry James G

Abstract excerpt

The crystal structure of Cam, the prototypic gamma-class carbonic anhydrase, reveals active site residues Gln75, Asn73, and Asn 202 previously hypothesized to participate in catalysis. These potential roles were investigated for the first time by kinetic analyses of site-specific replacement variants of the zinc and cobalt forms of Cam. Gln75 replacement variants showed large decreases in k(cat)/K(m) relative to...

Topics

Asparagine
Binding Sites
Carbonic Anhydrases
Glutamine
Hydrogen Bonding
Hydrogen-Ion Concentration
Kinetics
Models, Molecular
Mutation
Protein Structure, Tertiary
Spectrum Analysis

Source

Open in PubMed

Identifiers

PMID: 16618104
DOI: 10.1021/bi052507y

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics