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

Increasing the synthesis/hydrolysis ratio of aminoacylase 1 by site-directed mutagenesis.

Biochimie - 1 Jan 2010

Wardenga Rainer, Lindner Holger A, Hollmann Frank, Thum Oliver, Bornscheuer Uwe

Abstract excerpt

Aminoacylase-1 from pig kidney (pAcy1) catalyzes the highly stereoselective acylation of amino acids, a useful conversion for the preparation of optically pure N-acyl-l-amino acids. The kinetic of this thermodynamically controlled conversion is determined by maximal velocities for synthesis (V(mS)) and hydrolysis (V(mH)) of the N-acyl-l-amino acid. To investigate which parameter affects maximal velocities, we...

Topics

Acylation
Amidohydrolases
Amino Acids
Animals
Biocatalysis
Escherichia coli
Humans
Hydrolysis
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Nitrogen

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Sequence Homology, Amino Acid

Static Electricity

Swine

Source

Identifiers

PMID: 19818829
DOI: 10.1016/j.biochi.2009.09.017

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

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

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Increasing the synthesis/hydrolysis ratio of aminoacylase 1 by site-directed mutagenesis.PMID 19818829Read ↗

Probing the acyl-binding pocket of aminoacylase-1.Semantic proximity Read ↗

Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability.Semantic proximity Read ↗

Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation.Semantic proximity Read ↗

The molecular basis of aminoacylase 1 deficiency.Semantic proximity Read ↗

Characterization of Glu350 as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC 3.4.11.2): insights into its mechanism of action.Semantic proximity Read ↗

Improvement of the applicability of carboxypeptidase Y in peptide synthesis by protein engineering.Semantic proximity Read ↗

Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids.Semantic proximity Read ↗

Introduction of a C-terminal aromatic sequence from snake venom phospholipases A2 into the porcine pancreatic isozyme dramatically changes the interfacial kinetics.Semantic proximity Read ↗

The transmembrane tyrosines Y56, Y91 and Y167 play important roles in determining the affinity and transport rate of the rabbit proton-coupled peptide transporter PepT1.Semantic proximity Read ↗

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

Re-examining the role of Lys67 in class C beta-lactamase catalysis.Semantic proximity Read ↗

Site-directed mutation of arginine 282 to glutamate uncouples the movement of peptides and protons by the rabbit proton-peptide cotransporter PepT1.Semantic proximity Read ↗

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