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

Discovery of a new flavin N5-adduct in a tyrosine to phenylalanine variant of d-Arginine dehydrogenase.

Archives of biochemistry and biophysics - 15 Jan 2022

Iyer Archana, Reis Renata A G, Agniswamy Johnson, Weber Irene T, Gadda Giovanni

Abstract excerpt

d-Arginine dehydrogenase from Pseudomonas aeruginosa (PaDADH) catalyzes the flavin-dependent oxidation of d-arginine and other d-amino acids. Here, we report the crystal structure at 1.29 Å resolution for PaDADH-Y249F expressed and co-crystallized with d-arginine. The overall structure of PaDADH-Y249F resembled PaDADH-WT, but the electron density for the flavin cofactor was ambiguous, suggesting the presence of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Oxidoreductases
Share to Arginine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Flavin-Adenine Dinucleotide

Share to Guanidines

Share to Hydrogen Bonding

Share to Pseudomonas aeruginosa

Share to Static Electricity

Source

Identifiers

PMID: 34864048
DOI: 10.1016/j.abb.2021.109100

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Discovery of a new flavin N5-adduct in a tyrosine to phenylalanine variant of d-Arginine dehydrogenase.PMID 34864048Read ↗

An active site mutation induces oxygen reactivity in D-arginine dehydrogenase: A case of superoxide diverting protons.Semantic proximity Read ↗

Importance of Loop L1 Dynamics for Substrate Capture and Catalysis in Pseudomonas aeruginosa d-Arginine Dehydrogenase.Semantic proximity Read ↗

Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase.Semantic proximity Read ↗

Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa.Semantic proximity Read ↗

The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductaseSemantic proximity Read ↗

Members of the Rid protein family have broad imine deaminase activity and can accelerate the Pseudomonas aeruginosa D-arginine dehydrogenase (DauA) reaction in vitro.Semantic proximity Read ↗

Probing the function of a ligand-modulated dynamic tunnel in bifunctional proline utilization A (PutA).Semantic proximity Read ↗

Reconstructing a flavodoxin oxidoreductase with early amino acids.Semantic proximity Read ↗

Development of a Protein Scaffold for Arginine Sensing Generated through the Dissection of the Arginine-Binding Protein from Thermotoga maritima.Semantic proximity Read ↗

Y25S variant of Paracoccus pantotrophus cytochrome cd1 provides insight into anion binding by d1 heme and a rare example of a critical difference between solution and crystal structures.Semantic proximity Read ↗

The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3.Semantic proximity Read ↗

Engineering the substrate specificity of D-amino-acid oxidase.Semantic proximity Read ↗

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