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

Protein engineering of nitrile hydratase activity of papain: molecular dynamics study of a mutant and wild-type enzyme.

Journal of the American Chemical Society - 6 Nov 2002

Reddy Swarnalatha Y, Kahn Kalju, Zheng Ya-Jun, Bruice Thomas C

Abstract excerpt

The mechanism of hydrolysis of the nitrile (N-acetyl-phenylalanyl-2-amino-propionitrile, I) catalyzed by Gln19Glu mutant of papain has been studied by nanosecond molecular dynamics (MD) simulations. MD simulations of the complex of mutant enzyme with I and of mutant enzyme covalently attached to both neutral (II) and protonated (III) thioimidate intermediates were performed. An MD simulation with the wild-type...

Read the complete abstract on PubMed

Topics

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

Share to Computer Simulation
Share to Hydro-Lyases

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

Share to Nitriles

Share to Papain

Share to Phenylalanine

Share to Protein Conformation

Share to Protein Engineering

Share to Thermodynamics

Source

Identifiers

PMID: 12405824
DOI: 10.1021/ja020918l

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

Protein engineering of nitrile hydratase activity of papain: molecular dynamics study of a mutant and wild-type enzyme.PMID 12405824Read ↗

Is strong hydrogen bonding in the transition state enough to account for the observed rate acceleration in a mutant of papain?Semantic proximity Read ↗

3D Variability Analysis Reveals a Hidden Conformational Change Controlling Ammonia Transport in Human Asparagine SynthetaseSemantic proximity Read ↗

The natural mutation by deletion of Lys9 in the thrombin A-chain affects the pKa value of catalytic residues, the overall enzyme's stability and conformational transitions linked to Na+ binding.Semantic proximity Read ↗

Allosteric Breakage of the Hydrogen Bond within the Dual-Histidine Motif in the Active Site of Human Pin1 PPIase.Semantic proximity Read ↗

Kinetic, spectroscopic, and X-ray crystallographic characterization of the functional E151H aminopeptidase from Aeromonas proteolytica.Semantic proximity Read ↗

A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain.Semantic proximity Read ↗

Mechanism of 150-cavity formation in influenza neuraminidaseSemantic proximity Read ↗

The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenase.Semantic proximity Read ↗

Ammonium transport proteins with changes in one of the conserved pore histidines have different performance in ammonia and methylamine conduction.Semantic proximity Read ↗

Functional role of Asp160 and the deprotonation mechanism of ammonium in the Escherichia coli ammonia channel protein AmtB.Semantic proximity Read ↗

Kinetic and structural studies on roles of the serine ligand and a strictly conserved tyrosine residue in nitrile hydratase.Semantic proximity Read ↗

Analyzing the catalytic role of active site residues in the Fe-type nitrile hydratase from Comamonas testosteroni Ni1.Semantic proximity Read ↗

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