DAOA

Last update 08 May 2025

Basic Info

Synonyms

D-amino acid oxidase activator, DAOA, G72

+ [1]

Introduction

May suppress DAO (D-amino acid oxidase) and SOD1 activity and promote their degradation (PubMed:18544534, PubMed:20521334, PubMed:21679769, PubMed:30037290). Has conversely also been suggested to function as a DAO activator (PubMed:12364586, PubMed:24362575, PubMed:29114206). May stimulate the degradation of DDO (D-aspartate oxidase) (PubMed:37805834). May play a role in mitochondrial fission (PubMed:17684499).

100 Clinical Results associated with DAOA

100 Translational Medicine associated with DAOA

0 Patents (Medical) associated with DAOA

226

Literatures (Medical) associated with DAOA

12 Mar 2025·Journal of the American Chemical Society

Probing the Dynamics of Yersinia Adhesin A (YadA) in Outer Membranes Hints at Requirements for β-Barrel Membrane Insertion

Article

Author: Gumbart, James C. ; Ryoo, David ; Habeck, Michael ; Linke, Dirk ; Orwick-Rydmark, Marcella ; van Rossum, Barth-Jan ; Hofstetter, Albert ; Oschkinat, Hartmut ; Yarava, Jayasubba Reddy

The vast majority of cells are protected and functionalized by a dense surface layer of glycans, proteoglycans, and glycolipids. This surface represents an underexplored space in structural biology that is exceedingly challenging to recreate in vitro. Here, we investigate β-barrel protein dynamics within an asymmetric outer membrane environment, with the trimeric autotransporter Yersinia adhesin A (YadA) as an example. Magic-angle spinning NMR relaxation data and a model-free approach reveal increased mobility in the second half of strand β2 after the conserved G72, which is responsible for membrane insertion and autotransport, and in the subsequent loop toward β3. In contrast, the protomer-protomer interaction sites (β1_i-β4_i-1) are rigid. Intriguingly, the mobility in the β-strand section following G72 is substantially elevated in the outer membrane and less so in the detergent environment of microcrystals. A possible source is revealed by molecular dynamics simulations that show the formation of a salt bridge involving E79 and R76 in competition with a dynamic interplay of calcium binding by E79 and the phosphate groups of the lipids. An estimation of overall barrel motion in the outer membrane and detergent-containing crystals yields values of around 41 ns for both. The global motion of YadA in the outer membrane has a stronger rotational component orthogonal to the symmetry axis of the trimeric porin than in the detergent-containing crystal. In summary, our investigation shows that the mobility in the second half of β2 and the loop to β3 required for membrane insertion and autotransport is maintained in the final folded form of YadA.

01 Dec 2024·Biomolecular NMR Assignments

NMR-based solution structure of the Caulobacter crescentus ProXp-ala trans-editing enzyme

Article

Author: Musier-Forsyth, Karin ; Nagy, Alexandra B Kuzmishin ; Ma, Xiao ; Danhart, Eric M ; Duran, Antonia D ; Foster, Mark P

AbstractProXp-ala is a key component of the translational machinery in all three Domains of life. This enzyme helps to maintain the fidelity of proline codon translation through aminoacyl-tRNAPro proofreading. In the first step of tRNA aminoacylation, the cognate aminoacyl-tRNA synthetase (aaRS) binds and activates an amino acid in the enzyme’s synthetic active site. If a non-cognate amino acid passes this first selection step and is charged onto the tRNA, a distinct aaRS editing active site may recognize the mischarged tRNA and deacylate it. Alternatively, this editing reaction may be carried out by a separate enzyme that deacylates the mischarged tRNA in trans. ProXp-ala is responsible for editing Ala mischarged onto tRNAPro. Since trans-editing domains such as ProXp-ala bind their substrates after release from the synthetase, they must recognize not only the mischarged amino acid, but also the specific tRNA. Previous studies showed that Caulobacter crescentus (Cc) ProXp-ala distinguishes tRNAPro from tRNAAla, in part, based on the unique tRNAPro acceptor stem base pair C1:G72. Previous crystallographic and NMR data also revealed a role for conformational selection by the ProXp-ala α2 helix in Ala- versus Pro-tRNAPro substrate discrimination. The α2 helix makes lattice contacts in the crystal, which left some uncertainty as to its position in solution. We report resonance assignments for the substrate-free Cc ProXp-ala and the NMR-derived three-dimensional structure of the protein. These data reveal the position of the α2 helix in solution, with implications for substrate binding and recognition.

01 Oct 2024·Journal of Psychiatric Research

Plasma G72 protein in schizophrenia: A comparative analysis of drug-naive schizophrenia patients, patients in acute exacerbation and healthy controls

Article

Author: Kaya, Hasan ; Göka, Erol ; Fırat Oğuz, Esra ; Turhan, Turan ; Çiftçi, Hatice ; Aşut, Gonca ; Aydıner Yılmaz, Meltem ; Bayram, Şenol

OBJECTIVESSchizophrenia is a complex psychiatric disorder with an unclear etiopathogenesis. This study investigates the plasma G72 protein levels in drug-naive schizophrenia patients (DNS), those in acute psychotic episodes (AES), and healthy controls (HC). It also examines the correlation between the plasma G72 protein levels and Positive and Negative Syndrome Scale (PANSS) scores.METHODSThe study included 138 schizophrenia patients (84 DNS, 54 AES) and 83 HCs. Plasma G72 protein levels were measured by ELISA. Statistical analyses, including log-transformation and correlation analysis, were conducted.RESULTSSchizophrenia patients had significantly lower plasma G72 levels than HCs (4.39 ± 5.38 vs. 8.06 ± 10.27 ng/mL, p < 0.001), while DNS and AES groups did not differ significantly. Log-transformed data confirmed these differences. Negative correlation was found between plasma G72 levels and age (r = -0.258, p = 0.02), PANSS-G (r = -0.249, p = 0.004), and total PANSS scores (r = -0.226, p = 0.008). ROC analysis showed poor discrimination between schizophrenia patients and controls (AUC: 0.587, p = 0.031).CONCLUSIONSThis study's novel findings reveal that plasma G72 protein levels are significantly lower in schizophrenia patients and inversely correlated with age and symptom severity. However, the poor diagnostic accuracy observed in the ROC analysis suggests that G72 may not be a reliable biomarker for schizophrenia at this stage. These results underscore the need for further research to explore the potential clinical implications of these findings.

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DAOA

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