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

Mutational analysis of phenolic acid decarboxylase from Enterobacter sp. Px6-4. towards enhancement of binding affinity: A computational approach.

Computational biology and chemistry - 1 Oct 2018

Kumar Pravin, Kumari Priya, Sachan Shashwati Ghosh, Poddar Raju

Abstract excerpt

Microbial Ferulic Acid Decarboxylase (FADase) catalyses the conversion of ferulic acid to 4-hydroxy-3-methoxystyrene (4-vinylguaiacol) via non-oxidative decarboxylation. In this article, we present a computational, three-dimensional structural and functional analysis of FADase from Enterobacter sp. P × 6-4 (3NX1) which can be used to generate enhanced bindings of substrates. The enzymatic catalytic site and...

Read the complete abstract on PubMed

Topics

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

Share to Carboxy-Lyases
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Coumaric Acids

Share to DNA Mutational Analysis

Share to Enterobacter

Share to Hydrogen Bonding

Share to Molecular Docking Simulation

Share to Principal Component Analysis

Source

Identifiers

PMID: 30081341
DOI: 10.1016/j.compbiolchem.2018.06.004

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Mutational analysis of phenolic acid decarboxylase from Enterobacter sp. Px6-4. towards enhancement of binding affinity: A computational approach.PMID 30081341Read ↗

Enhancement of the catalytic activity of ferulic acid decarboxylase from Enterobacter sp. Px6-4 through random and site-directed mutagenesis.Semantic proximity Read ↗

Structure and Mechanism of Ferulic Acid Decarboxylase (FDC1) from Saccharomyces cerevisiae.Semantic proximity Read ↗

The novel R347g pathogenic mutation of aromatic amino acid decarboxylase provides additional molecular insights into enzyme catalysis and deficiency.Semantic proximity Read ↗

Molecular docking and simulation study for synthesis of alternative dapsone derivative as a newer antileprosy drug in multidrug therapy.Semantic proximity Read ↗

Improving the Thermostability of Xylanase A from Bacillus subtilis by Combining Bioinformatics and Electrostatic Interactions Optimization.Semantic proximity Read ↗

Analysis of the Effect of N555 Mutations on the Product Specificity of Dextransucrase Using Caffeic Acid Phenethyl Ester as an Acceptor Substrate.Semantic proximity Read ↗

Homology modeling and protein engineering of alkane monooxygenase in Burkholderia thailandensis MSMB121: in silico insights.Semantic proximity Read ↗

Enhancing the specific activity of 3α-hydroxysteroid dehydrogenase through cross-regional combinatorial mutagenesis.Semantic proximity Read ↗

Integrated computer-aided drug design and biophysical simulation approaches to determine natural anti-bacterial compounds for Acinetobacter baumanniiSemantic proximity Read ↗

An evolution-based designing and characterization of mutants of cyclomaltodextrinase: Molecular modeling and spectroscopic studies.Semantic proximity Read ↗

Improving the thermal stability and catalytic activity of ulvan lyase by the combination of FoldX and KnowVolution campaign.Semantic proximity Read ↗

Distal mutations enhance efficiency of free and immobilized NOV1 dioxygenase for vanillin synthesis.Semantic proximity Read ↗

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