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

Structures of the catalytic site mutants D99A and H48Q and the calcium-loop mutant D49E of phospholipase A2.

Acta crystallographica. Section D, Biological crystallography - 1 Feb 1999

Sekar K, Biswas R, Li Y, Tsai M, Sundaralingam M

Abstract excerpt

Crystal structures of the active-site mutants D99A and H48Q and the calcium-loop mutant D49E of bovine phospholipase A2 have been determined at around 1.9 A resolution. The D99A mutant is isomorphous to the orthorhombic recombinant enzyme, space group P212121. The H48Q and the calcium-loop mutant D49E are isomorphous to the trigonal recombinant enzyme, space group P3121. The two active-site mutants show no major...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Catalytic Domain
Share to Cattle

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

Share to Crystallography, X-Ray

Share to Hydrogen Bonding

Share to Mutation

Share to Phospholipases A

Share to Phospholipases A2

Source

Identifiers

PMID: 10089353
DOI: 10.1107/s0907444998013699

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structures of the catalytic site mutants D99A and H48Q and the calcium-loop mutant D49E of phospholipase A2.PMID 10089353Read ↗

Structures and molecular-dynamics studies of three active-site mutants of bovine pancreatic phospholipase A(2).Semantic proximity Read ↗

Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase.Semantic proximity Read ↗

A redetermination of the structure of the triple mutant (K53,56,120M) of phospholipase A2 at 1.6 A resolution using sulfur-SAS at 1.54 A wavelength.Semantic proximity Read ↗

Structural analysis of the two horseradish peroxidase catalytic residue variants H42E and R38S/H42E: implications for the catalytic cycle.Semantic proximity Read ↗

Active site mutant Glu-43----Asp in staphylococcal nuclease displays nonlocal structural changes.Semantic proximity Read ↗

Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase.Semantic proximity Read ↗

Crystal structures of the apo- and holomutant human lysozymes with an introduced Ca2+ binding site.Semantic proximity Read ↗

Functional importance of calcium binding sites in outer membrane phospholipase A.Semantic proximity Read ↗

Human recombinant alpha-parvalbumin and nine mutants with individually inactivated calcium- and magnesium-binding sites: biochemical and immunological properties.Semantic proximity Read ↗

Symmetrical stabilization of bound Ca2+ ions in a cooperative pair of EF-hands through hydrogen bonding of coordinating water molecules in calbindin D(9k).Semantic proximity Read ↗

Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants.Semantic proximity Read ↗

Crystal structure of the O intermediate of the Leu93→Ala mutant of bacteriorhodopsin.Semantic proximity Read ↗

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