DERA

Last update 08 May 2025

Basic Info

Synonyms

2-deoxy-D-ribose 5-phosphate aldolase, CGI-26, DEOC

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Introduction

Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. Participates in stress granule (SG) assembly. May allow ATP production from extracellular deoxyinosine in conditions of energy deprivation.

100 Clinical Results associated with DERA

100 Translational Medicine associated with DERA

0 Patents (Medical) associated with DERA

163

Literatures (Medical) associated with DERA

07 Mar 2025·The Journal of Organic Chemistry

Enantiodivergent Synthesis of Both (R)- and (S)-Heteroaryl Aldols by Rationally Engineered Aldolases

Article

Author: Naik, Karishma ; Bar, Krishnendu ; Jeevani, Kodru ; Saravanan, Thangavelu

Aldolases, especially 2-deoxyribose-5-phosphate aldolase (DERA) enzymes, have been widely employed to access key chiral precursors for various active pharmaceutical ingredients (APIs). This has been enabled by expanding their substrate scope toward non-natural acceptors and donors via protein engineering. In this study, we endeavored to broaden the acceptor substrate scope of DERA from Geobacillus sp. (DERA_Geo) toward the heteroaryl aldehydes through a rational protein engineering approach. We successfully performed iterative saturation mutagenesis of DERA_Geo, resulting in two enantiocomplementary variants, viz., (R)-selective DERA_Geo-S185G and (S)-selective DERA_Geo-T12I/S185A, with enhanced catalytic efficiencies and enantioselectivities. Remarkably, the natural enantioselectivity of DERA_Geo was reversed by a single mutation (S185G). The synthetic applicability of the mutants was demonstrated by conducting aldol reactions on a semipreparative scale, from which both (R)- and (S)-enantiomers of heteroaryl aldols were isolated with high yields (up to 99%) and excellent enantiopurities (up to 99:1 e.r.).

01 Oct 2024·Neurobiology of Disease

The proteomic signature of circulating extracellular vesicles following intracerebral hemorrhage: Novel insights into mechanisms underlying recovery

Article

Author: Bravo, Susana-Belén ; de Leciñana, María Alonso ; Alonso-López, Elisa ; Otero-Ortega, Laura ; de Frutos, Mari-Carmen Gómez ; Laso-García, Fernando ; de Celis-Ruiz, Elena ; Piniella, Dolores ; Casado-Fernández, Laura ; Alonso de Leciñana, María ; Hervás, Carlos ; Rigual, Ricardo ; Ruiz-Ares, Gerardo ; Gómez-de Frutos, Mari Carmen ; Rodríguez-Pardo, Jorge ; Docando, Félix ; Fuentes-Gimeno, Blanca ; Gutiérrez-Fernández, María ; Díez-Tejedor, Exuperio

Circulating extracellular vesicles (EVs) can participate in innate repair processes triggered after intracerebral hemorrhage (ICH). We aimed to describe changes in the proteomic profile of circulating EVs between the acute and subacute phases of ICH and to compare the findings depending on outcomes, as an approach to unraveling such repair mechanisms. This was a prospective observational study including patients with non-traumatic supratentorial ICH. Exclusion criteria were previous disability, signs of herniation on baseline computed tomography, or limited life expectancy. EVs were isolated from blood samples at 24 h and 7 days after symptom onset. After 6-months' follow-up, patients were dichotomized into poor and good outcomes, defining good as an improvement of >10 points or > 50 % on the National Institutes of Health Stroke Scale and a modified Rankin Scale of 0-2. The protein cargo was analyzed by quantitative mass spectrometry and compared according to outcomes. Forty-four patients completed follow-up, 16 (35.5 %) having good outcomes. We identified 1321 proteins in EVs, 37 with differential abundance. In patients with good outcomes, proteins related to stress response (DERA, VNN2, TOMM34) and angiogenesis (RHG01) had increased abundance at 7 days. EVs from patients with poor outcomes showed higher levels of acute-phase reactants (CRP, SAA2) at 7 days compared with 24 h. In conclusion, the protein content of circulating EVs in patients with ICH changes over time, the changes varying depending on the clinical outcome, with greater abundance of proteins potentially involved in the repair processes of patients with good outcomes.

21 Aug 2024·Applied and Environmental Microbiology

An aldolase-dependent phloroglucinol degradation pathway in Collinsella sp. zg1085

Article

Author: Tu, Yanqin ; Li, Tong ; Xu, Tong ; Li, Yating ; Wei, Yifeng ; Zhou, Yan

ABSTRACT Phloroglucinol (1,3,5-trihydroxybenzene) is a key intermediate in the degradation of polyphenols such as flavonoids and hydrolysable tannins and can be used by certain bacteria as a carbon and energy source for growth. The identification of enzymes that participate in the fermentation of phloroglucinol to acetate and butyrate in Clostridia was recently reported. In this study, we present the discovery and characterization of a novel metabolic pathway for phloroglucinol degradation in the bacterium Collinsella sp. zg1085, from marmot respiratory tract. In both the Clostridial and Collinsella pathways, phloroglucinol is first reduced to dihydrophoroglucinol by the NADPH-dependent phloroglucinol reductase (PGR), followed by ring opening to form ( S )-3-hydroxy-5-oxohexanoate by a Mn 2+ -dependent dihydrophloroglucinol cyclohydrolase (DPGC). In the Collinsella pathway, ( S )-3-hydroxy-5-oxohexanoate is then cleaved to form malonate semialdehyde and acetone by a newly identified aldolase (HOHA). Finally, a NADP + -dependent malonate-semialdehyde dehydrogenase converts malonate semialdehyde to CO 2 and acetyl-CoA, an intermediate in carbon and energy metabolism. Recombinant expression of the Collinsella PGR, DPGC, and HOHA in E. coli enabled the conversion of phloroglucinol into acetone, providing support for the proposed pathway. Experiments with Olsenella profusa , another bacterium containing the gene cluster of interest, show that the PGR, DPGC, HOHA, and MSDH are induced by phloroglucinol. Our findings add to the variety of metabolic pathways for the degradation of phloroglucinol, a widely distributed phenolic compound, in the anaerobic microbiome. IMPORTANCE Phloroglucinol is an important intermediate in the bacterial degradation of polyphenols, a highly abundant class of plant natural products. Recent research has identified key enzymes of the phloroglucinol degradation pathway in butyrate-producing anaerobic bacteria, which involves cleavage of a linear triketide intermediate by a beta ketoacid cleavage enzyme, requiring acetyl-CoA as a co-substrate. This paper reports a variant of the pathway in the lactic acid bacterium Collinsella sp. zg1085, which involves cleavage of the triketide intermediate by a homolog of deoxyribose-5-phosphate aldolase, highlighting the variety of mechanisms for phloroglucinol degradation by different anaerobic bacterial taxa.

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