DCTD

Last update 08 May 2025

Basic Info

Synonyms

dCMP deaminase, DCTD, Deoxycytidylate deaminase

Introduction

Catalyzes the deamination of dCMP to dUMP, providing the nucleoside monophosphate substrate for the thymidylate synthase/TYMS (PubMed:7685356). Also, part of a nucleotide salvage pathway that eliminates epigenetically modified 5-hydroxymethyl-dCMP (hmdCMP) in a two-step process entailing deamination to cytotoxic 5-hydroxymethyl-dUMP (hmdUMP), followed by its hydrolysis into 5-hydroxymethyluracil (hmU) and 2-deoxy-D-ribose 5-phosphate (deoxyribosephosphate) (PubMed:33833118). Catalyzes the first step in that pathway, the deamination of 5-hydroxymethyl-dCMP (hmdCMP) (PubMed:33833118).

100 Clinical Results associated with DCTD

100 Translational Medicine associated with DCTD

0 Patents (Medical) associated with DCTD

375

Literatures (Medical) associated with DCTD

01 Aug 2025·Microbial Pathogenesis

dctA, dctB, and dctD contribute to the utilization of C4-dicarboxylates, carbon, nitrogen, as well as virulence in Acidovorax citrulli

Article

Author: Mijiti, Maihemuti ; Zhao, Tingchang ; Yang, Yuwen ; Guan, Wei ; Yang, Lina ; Abuduzhayier, Ayijiamali ; Wang, Lan

Bacterial fruit blotch (BFB), a destructive bacterial disease triggered by Acidovorax citrulli, affects cucurbit crops like watermelon and melon. The absorption and use of carbon sources are foundational for bacteria to successfully colonize host plants. C4-dicarboxylates are critical carbon and energy substances, and their transport is completed by the C4-dicarboxylate transport system (Dct) which plays an important role in typical bacterial metabolism. However, the role of dct genes have not been determined for A. citrulli. To clarify the biological roles of the Dct system-related genes in A. citrulli, we developed dctA1, dctA2, dctB, and dctD deletion mutants, as well as dctA1A2 double deletion mutant, with their corresponding complementary strains in the A. citrulli wild-type strain Aac5 in this study. The functions of Dct-related genes in A. citrulli were analyzed through phenotype assays, including pathogenicity, C4-dicarboxylates utilization, carbon and nitrogen utilization, biofilm formation, swimming motility, and qRT-PCR analysis. Compared to the wild-type strain, the pathogenicity, utilization of C4-dicarboxylates, growth ability in vivo and in vitro, and seed adhesion ability of the mutant strains were significantly limited, while the biofilm formation ability was significantly improved. Additionally, the utilization of select carbon sources (glucose, maltose, and sucrose) and nitrogen sources ((NH₄)₂SO₄, NH₄Cl, CH₄N₂O, and KNO₃) was significantly enhanced. qRT-PCR results demonstrated that the deletion of Dct-related genes resulted in significant downregulation of the expression of T3SS-related genes (hrpG and hrpE), the pili-related genes (pilA and pilN), and some flagellum-related genes (fliC, flhC, and flhD). These findings suggested that Dct-related genes were involved in C4-dicarboxylate utilization, carbon and nitrogen use, and the pathogenicity of A. citrulli.

22 Apr 2025·Proceedings of the National Academy of Sciences

An integrated mechanism of G _q regulation of PLCβ enzymes

Article

Author: Lu, Sumin ; Jang, Wonjo ; Lyon, Angeline M. ; Lambert, Nevin A. ; Fisher, Isaac J. ; Senarath, Kanishka ; Kostenis, Evi ; Inoue, Asuka

Phospholipase Cβ (PLCβ) enzymes are the principal effectors activated by G q heterotrimers. Both Gα q and Gβγ subunits can activate PLCβ, which requires precise positioning of PLCβ at the plasma membrane to relieve structural autoinhibition and give the active site access to the phosphatidylinositol 4,5-bisphosphate (PIP2) substrate. PLCβ enzymes possess a unique distal C-terminal domain (dCTD) that is critical for activation by Gα q , but the reason for this is unclear. It is also not known how G protein activation affects the subcellular localization of PLCβ enzymes, some of which are found primarily in the cytosol despite needing to act at the plasma membrane. Here, we use bioluminescence spectroscopy, imaging, and gene editing to study the membrane disposition of PLCβ enzymes in living cells and to define the functional roles of the dCTD. We find that PLCβ translocates to the plasma membrane upon G q activation, primarily by binding to Gα q subunits. This is rapidly counteracted by PIP2 hydrolysis, which promotes PLCβ translocation back into the cytosol. PLCβ translocation and activation require binding of Gα q to the catalytic domain and the dCTD at two distinct interfaces. Gα q binding to the dCTD is required for activation even when PLCβ is artificially tethered to the plasma membrane, suggesting that this domain has functions beyond simply recruiting the enzyme to the PIP2 substrate. We propose that in addition to associating PLCβ with the plasma membrane, the dCTD reorders the αN helix of active Gα q and thus participates directly in the precise positioning of the catalytic domain.

01 Mar 2025·Fish & Shellfish Immunology

Molecular responses of Mytilus coruscus hemocytes to lipopolysaccharide and peptidoglycan as revealed by 4D-DIA based quantitative proteomics analysis

Article

Author: Yang, Zilin ; Wu, Xiaoshan ; Zhang, Xiaolin ; Buttino, Isabella ; Wang, Yue ; Liao, Zhi ; Xiao, Wenhui ; Yan, Xiaojun ; Song, Fang ; He, Jianyu

Mytilus are sessile filter feeders that live in close contact with numerous marine microorganisms. Hemocytes, the immunocompetent cells of Mytilus, participate in the immune response in a very efficient manner. Lipopolysaccharide (LPS) and peptidoglycan (PGN) follow specific microbe/pathogen-associated molecular patterns (MAMPs or PAMPs) and are involved in immune stimulation in host cells. This study evaluated the molecular profiles and reactions at protein level of Mytilus hemocytes after stimulation with LPS and PGN. Mytilus coruscus was challenged in vivo with LPS and PGN. The hemocytes were collected after 48 h and analyzed for quantitative proteomics, cell subpopulations, and the free amino acid composition. 4D-DIA technology-based proteomic analysis revealed different protein profiles, as well as different responses at protein level, under either the LPS or PGN challenge. C-type lectins, collagens, and CD151 protein were highly upregulated in LPS-challenged mussels, while phospholipase A2 and dCMP deaminase were highly upregulated in PGN-challenged mussels. Moreover, LPS challenge disrupted dsRNA-mediated translation and stimulated energy-related metabolism, while PGN challenge stimulated proteins involved in the inflammatory response and suppressed amino acid metabolism. In addition, the LPS and PGN challenges differed in their effects on the free amino acid composition and granulocytes ratio of the hemocytes. These findings highlight the different strategies employed by mussel hemocytes in response to different MAMPs, providing insights into the effects of LPS and PGN on Mytilus.

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DCTD

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