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 modified flavins. Electron density maps and mass spectrometric analysis confirmed the presence of both N5-(4-guanidino-oxobutyl)-FAD and 6-OH-FAD in a single crystal of PaDADH-Y249F and helped with the further refinement of the X-ray crystal structure. The versatility of the reduced flavin is apparent in the PaDADH-Y249F structure and is evidenced by the multiple functions it can perform in the same active site.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.abb.2021.109100 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
An active site mutation induces oxygen reactivity in D-arginine dehydrogenase: A case of superoxide diverting protons.
J Biol Chem
June 2024
Department of Chemistry, Georgia State University, Atlanta, Georgia, USA; Department of Biology, Georgia State University, Atlanta, Georgia, USA; Department of the Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, Georgia, USA. Electronic address:
Enzymes are potent catalysts that increase biochemical reaction rates by several orders of magnitude. Flavoproteins are a class of enzymes whose classification relies on their ability to react with molecular oxygen (O) during catalysis using ionizable active site residues. Pseudomonas aeruginosa D-arginine dehydrogenase (PaDADH) is a flavoprotein that oxidizes D-arginine for P.
View Article and Find Full Text PDFGranulocyte pro-myeloperoxidase is redundantly processed by proprotein convertase furin and PC7 in HL-60 cells.
Biochem Cell Biol
June 2024
TransBIOTech, Lévis, QC G6V 6Z3, Canada.
Neutrophil myeloperoxidase/HO/chloride system is a key mechanism to control pathogen infection. This enzyme, myeloperoxidase, plays a pivotal role in the arsenal of azurophilic granules that are released through degranulation upon neutrophil activation, which trigger local hypochlorous acid production. Myeloperoxidase gene encodes a protein precursor named promyeloperoxidase that arbors a propeptide that gets cleaved later during secretory routing in post-endoplasmic reticulum compartments.
View Article and Find Full Text PDFFunctional characterization of the locus for D-branched-chain amino acid catabolism in .
Appl Environ Microbiol
February 2024
Department of Microbiology, University of Georgia, Athens, Georgia, USA.
is a metabolically robust soil bacterium that employs a diverse set of pathways to utilize a wide range of nutrients. The versatility of this microorganism contributes to both its environmental ubiquity and its rising popularity as a bioengineering chassis. In , the newly named locus encodes a transcriptional regulator (DbuR), D-amino acid oxidase (DbuA), Rid2 protein (DbuB), and a putative transporter (DbuC).
View Article and Find Full Text PDFTargeted Mutation of a Non-catalytic Gating Residue Increases the Rate of d-Arginine Dehydrogenase Catalytic Turnover.
J Agric Food Chem
November 2023
Department of Chemistry, Georgia State University, Atlanta, Georgia 30302-3965, United States.
Commercial food and l-amino acid industries rely on bioengineered d-amino acid oxidizing enzymes to detect and remove d-amino acid contaminants. However, the bioengineering of enzymes to generate faster biological catalysts has proven difficult as a result of the failure to target specific kinetic steps that limit enzyme turnover, , and the poor understanding of loop dynamics critical for catalysis. d-arginine dehydrogenase (DADH) oxidizes most d-amino acids and is a good candidate for application in the l-amino acid and food industries.
View Article and Find Full Text PDFPolydopamine-cloaked Fe-based metal organic frameworks enable synergistic multidimensional treatment of osteosarcoma.
J Colloid Interface Sci
December 2023
College of Biological Science and Medical Engineering, Donghua University, Shanghai 201620, China. Electronic address:
One of the major challenges in effective cancer therapy arises because of the hypoxic microenvironment in the tumor. This compromises the efficacy of both chemo- and radiotherapy, and thus hinders patient outcomes. To solve this problem, we constructed polydopamine (PDA)-cloaked Fe-based metal organic frameworks (MOFs) loaded with d-arginine (d-Arg), glucose oxidase (GOX), and the chemotherapeutic drug tirapazamine (TPZ).
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!