Discover Community Create You

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

Article

Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II.

The Journal of biological chemistry - 25 Dec 1993

Krebs J F, Ippolito J A, Christianson D W, Fierke C A

Abstract excerpt

Amino acid substitutions at Thr199 of human carbonic anhydrase II (CAII) (Thr199-->Ser, Ala, Val, and Pro) were characterized to investigate the importance of a conserved hydrogen bonding network. The three-dimensional structures of azide-bound and sulfate-bound T199V CAIIs were determined by x-ray crystallographic methods at 2.25 and 2.4 A, respectively (final crystallographic R factors are 0.173 and 0.174,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Carbon Dioxide
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Esterases

Share to Hydrogen Bonding

Share to Mutation

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 8262987

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II.PMID 8262987Read ↗

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

Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-.Semantic proximity Read ↗

Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III.Semantic proximity Read ↗

Proton transfer in a Thr200His mutant of human carbonic anhydrase II.Semantic proximity Read ↗

Comparative study of stability and activity of wild-type and mutant human carbonic anhydrase II enzymes using molecular dynamics and docking simulations.Semantic proximity Read ↗

Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase II.Semantic proximity Read ↗

Activation of carbonic anhydrase II by active-site incorporation of histidine analogs.Semantic proximity Read ↗

Structural Characterization of Carbonic Anhydrase VIII and Effects of Missense Single Nucleotide Variations to Protein Structure and Function.Semantic proximity Read ↗

Fine tuning of the catalytic properties of carbonic anhydrase. Studies of a Thr200----His variant of human isoenzyme II.Semantic proximity Read ↗

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

H, 15 N and 13 C resonance assignments of S2A and H64A double mutant of human carbonic anhydrase IISemantic proximity Read ↗

Directed Evolution of the Promiscuous Esterase Activity of Carbonic Anhydrase IISemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.