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

X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis.

Biochemistry - 24 Dec 1996

Scolnick L R, Christianson D W

Abstract excerpt

The three-dimensional structures of A65F, A65L, A65H, A65T, A65S, and A65G human carbonic anhydrase II (CAII) variants have been solved by X-ray crystallographic methods to probe the importance of residue 65 and the structural implications of its evolutionary drift in the greater family of carbonic anhydrase isozymes. Structure-activity relationships in this series of CAII variants are correlated with those...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Evolution, Molecular
Share to Genetic Variation

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

Share to In Vitro Techniques

Share to Models, Molecular

Share to Molecular Structure

Share to Protein Conformation

Share to Recombinant Proteins

Source

Identifiers

PMID: 8987974
DOI: 10.1021/bi9617872

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

X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis.PMID 8987974Read ↗

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

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

1H, 15N and 13C resonance assignments of the S2A and H64A double mutant of human carbonic anhydrase II.Semantic proximity Read ↗

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

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

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

Proton transfer pathways in the mutant His-64-Ala of human carbonic anhydrase II.Semantic proximity Read ↗

Structural insights into a thermostable variant of human carbonic anhydrase II.Semantic proximity Read ↗

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

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

A structure-function study of a proton transport pathway in the gamma-class carbonic anhydrase from Methanosarcina thermophila.Semantic proximity Read ↗

Water-Restructuring Mutations Can Reverse the Thermodynamic Signature of Ligand Binding to Human Carbonic Anhydrase.Semantic proximity Read ↗

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