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

Thermodynamic profiles of penicillin G hydrolysis catalyzed by wild-type and Met----Ala168 mutant penicillin acylases from Kluyvera citrophila.

Biochimica et biophysica acta - 9 Feb 1990

Martín J, Prieto I, Barbero J L, Pérez-Gil J, Mancheño J M, Arche R

Abstract excerpt

The Met-168 residue in penicillin acylase from Kluyvera citrophila was changed to Ala by oligonucleotide site-directed mutagenesis. The Ala-168 mutant exhibited different substrate specificity than wild-type and enhanced thermal stability. The thermodynamic profiles for penicillin G hydrolysis catalyzed by both enzymes were obtained from the temperature dependence of the steady-state kinetic parameters Km and...

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 Hydrogen-Ion Concentration

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

Share to Hydrolysis

Share to Kinetics

Share to Mutation

Share to Protein Conformation

Share to Substrate Specificity

Share to Thermodynamics

Source

Identifiers

PMID: 2306469
DOI: 10.1016/0167-4838(90)90158-c

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

Thermodynamic profiles of penicillin G hydrolysis catalyzed by wild-type and Met----Ala168 mutant penicillin acylases from Kluyvera citrophila.PMID 2306469Read ↗

Structure mediation in substrate binding and post-translational processing of penicillin acylases: Information from mutant structures of Kluyvera citrophila penicillin G acylase.Semantic proximity Read ↗

Rapid burst kinetics in the hydrolysis of 4-nitrophenyl acetate by penicillin G acylase from Kluyvera citrophila. Effects of mutation F360V on rate constants for acylation and de-acylation.Semantic proximity Read ↗

On the functional role of Arg172 in substrate binding and allosteric transition in Escherichia coli glucosamine-6-phosphate deaminase.Semantic proximity Read ↗

Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding.Semantic proximity Read ↗

Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies.Semantic proximity Read ↗

Cloning, overexpression, crystallization and preliminary X-ray crystallographic analysis of a slow-processing mutant of penicillin G acylase from Kluyvera citrophila.Semantic proximity Read ↗

Thermodynamic integration calculations of binding free energy difference for Gly-169 mutation in subtilisin BPN'.Semantic proximity Read ↗

Site-directed mutagenesis studies of the aromatic residues at the active site of a lipase from Malassezia globosa.Semantic proximity Read ↗

Structural and kinetic studies on ligand binding in wild-type and active-site mutants of penicillin acylase.Semantic proximity Read ↗

Improved A. faecalis penicillin amidase mutant retains the thermodynamic and pH stability of the wild type enzyme.Semantic proximity Read ↗

Role of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site.Semantic proximity Read ↗

Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori.Semantic proximity Read ↗

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