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    Cdo1 cysteine dioxygenase 1, cytosolic [ Mus musculus (house mouse) ]

    Gene ID: 12583, updated on 23-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Cdo1-Camkk2-AMPK axis confers the protective effects of exercise against NAFLD in mice.

    Cdo1-Camkk2-AMPK axis confers the protective effects of exercise against NAFLD in mice.
    Chen M, Zhu JY, Mu WJ, Luo HY, Li Y, Li S, Yan LJ, Li RY, Guo L., Free PMC Article

    01/3/2024
    Cdo1 promotes PPARgamma-mediated adipose tissue lipolysis in male mice.

    Cdo1 promotes PPARγ-mediated adipose tissue lipolysis in male mice.
    Guo YY, Li BY, Xiao G, Liu Y, Guo L, Tang QQ.

    10/29/2022
    findings suggest that epididymal CDO plays a key role in post-testicular sperm maturation, enabling sperm to osmoregulate as they transition from the male to the female reproductive tract

    Cysteine dioxygenase is essential for mouse sperm osmoadaptation and male fertility.
    Asano A, Roman HB, Hirschberger LL, Ushiyama A, Nelson JL, Hinchman MM, Stipanuk MH, Travis AJ., Free PMC Article

    03/16/2019
    Presented here are the results of O2-dependent 2-mercaptoaniline reaction using two different thiol dioxygenase enzymes mouse CDO and 3-mercaptopropionic acid dioxygenase isolated from Azotobacter vinelandii. Benzothiazoles are produced by the condensation of 2-mercaptoaniline with aldehydes formed by an off-pathway oxidation of primary alcohols added to aqueous reactions to solubilize the substrate.

    Thiol dioxygenase turnover yields benzothiazole products from 2-mercaptoaniline and O(2)-dependent oxidation of primary alcohols.
    Morrow WP, Sardar S, Thapa P, Hossain MS, Foss FW Jr, Pierce BS., Free PMC Article

    09/23/2017
    Cdo is required for efficient cardiomyogenesis of pluripotent stem cells and an excellent target to improve the differentiation potential of stem cells for generation of transplantable cells to treat cardiomyopathies.

    A Shh coreceptor Cdo is required for efficient cardiomyogenesis of pluripotent stem cells.
    Jeong MH, Leem YE, Kim HJ, Kang K, Cho H, Kang JS.

    06/3/2017
    our findings indicate Cdo1 suppresses osteogenic differentiation of BMSCs, through a potential mechanism which involves in Wnt signaling reduction concomitantly

    Cysteine Dioxygenase Type 1 Inhibits Osteogenesis by Regulating Wnt Signaling in Primary Mouse Bone Marrow Stromal Cells.
    Zhao X, Deng P, Feng J, Wang Z, Xiang Z, Han X, Bai D, Pae EK., Free PMC Article

    12/31/2016
    We investigated the ontogeny of Cdo1 mRNA expression in mouse fetal and placental tissues, which showed increasing levels from embryonic day 10.5 and was localised to the decidua and several fetal tissues including nasal cavities and brain.

    Placental and fetal cysteine dioxygenase gene expression in mouse gestation.
    Rakoczy J, Lee S, Weerasekera SJ, Simmons DG, Dawson PA.

    05/28/2016
    Cdo1 is required for adipogenesis.Cdo1 interacts with Ppar-gamma during adipogenesis.

    Cysteine dioxygenase type 1 promotes adipogenesis via interaction with peroxisome proliferator-activated receptor gamma.
    Deng P, Chen Y, Ji N, Lin Y, Yuan Q, Ye L, Chen Q.

    05/9/2015
    In light of these results, the minimal substrate requirements for CDO catalysis and O-activation are discussed.

    Steady-state substrate specificity and O₂-coupling efficiency of mouse cysteine dioxygenase.
    Li W, Pierce BS.

    03/21/2015
    the timing of chemical steps in the CDO kinetic mechanism is investigated by pH/pD-dependent steady-state kinetics and solvent isotope effects on kcat, kcat/KM, and (O2/CSA) coupling

    Oxidative uncoupling in cysteine dioxygenase is gated by a proton-sensitive intermediate.
    Crowell JK, Li W, Pierce BS.

    02/14/2015
    Cdo1 knockout mice show increased cysteine concentrations and higher rates of metabolism of cysteine to hydrogen sulfide and thiosulfate.

    Primary hepatocytes from mice lacking cysteine dioxygenase show increased cysteine concentrations and higher rates of metabolism of cysteine to hydrogen sulfide and thiosulfate.
    Jurkowska H, Roman HB, Hirschberger LL, Sasakura K, Nagano T, Hanaoka K, Krijt J, Stipanuk MH., Free PMC Article

    01/3/2015
    A critical function of CDO appears to be to remove cysteine by a pathway in which the sulfur atom is oxidized in the first step.

    The cysteine dioxgenase knockout mouse: altered cysteine metabolism in nonhepatic tissues leads to excess H2S/HS(-) production and evidence of pancreatic and lung toxicity.
    Roman HB, Hirschberger LL, Krijt J, Valli A, Kožich V, Stipanuk MH., Free PMC Article

    05/3/2014
    Data from kinetic, spectroscopic, and computational studies suggest that in cysteine dioxygenase (CDO) a covalently cross-linked cysteine-tyrosine pair (C93-Y157) plays a vital role in CDO-mediated catalysis.

    Second-sphere interactions between the C93-Y157 cross-link and the substrate-bound Fe site influence the O₂ coupling efficiency in mouse cysteine dioxygenase.
    Li W, Blaesi EJ, Pecore MD, Crowell JK, Pierce BS.

    03/8/2014
    Cdo(-/-) mice displayed megaesophagus and achalasia, and their lower esophageal sphincter was resistant to nitric oxide-induced relaxation.

    Smooth muscle fascicular reorientation is required for esophageal morphogenesis and dependent on Cdo.
    Romer AI, Singh J, Rattan S, Krauss RS., Free PMC Article

    06/15/2013
    The hepatic CDO-knockout mice were able to maintain normal levels of glutathione, taurine, and sulfate.

    Extrahepatic tissues compensate for loss of hepatic taurine synthesis in mice with liver-specific knockout of cysteine dioxygenase.
    Ueki I, Roman HB, Hirschberger LL, Junior C, Stipanuk MH., Free PMC Article

    07/21/2012
    The catalytic cycle of CDO is primed by one electron through chemical oxidation to produce CDO with ferric iron in the active site.

    Single turnover of substrate-bound ferric cysteine dioxygenase with superoxide anion: enzymatic reactivation, product formation, and a transient intermediate.
    Crawford JA, Li W, Pierce BS.

    02/11/2012
    Control of cysteine levels by regulation of CDO may be necessary to maintain low H(2)S/sulfane sulfur levels and facilitate the use of H(2)S as a signaling molecule.

    Knockout of the murine cysteine dioxygenase gene results in severe impairment in ability to synthesize taurine and an increased catabolism of cysteine to hydrogen sulfide.
    Ueki I, Roman HB, Valli A, Fieselmann K, Lam J, Peters R, Hirschberger LL, Stipanuk MH., Free PMC Article

    11/19/2011
    resting and substrate-bound forms of CDO in the Fe(II) and Fe(III) states, both of which are proposed to have important roles in this enzyme's catalytic mechanism, were characterized.

    Spectroscopic and computational characterization of substrate-bound mouse cysteine dioxygenase: nature of the ferrous and ferric cysteine adducts and mechanistic implications.
    Gardner JD, Pierce BS, Fox BG, Brunold TC., Free PMC Article

    08/30/2010
    Characterization of the nitrosyl adduct of substrate-bound mouse cysteine dioxygenase by electron paramagnetic resonance

    Characterization of the nitrosyl adduct of substrate-bound mouse cysteine dioxygenase by electron paramagnetic resonance: electronic structure of the active site and mechanistic implications.
    Pierce BS, Gardner JD, Bailey LJ, Brunold TC, Fox BG.

    01/21/2010
    The x-ray crystal structure of CDO from Mus musculus was solved to a nominal resolution of 1.75 Angstroms

    Structure and mechanism of mouse cysteine dioxygenase.
    McCoy JG, Bailey LJ, Bitto E, Bingman CA, Aceti DJ, Fox BG, Phillips GN Jr., Free PMC Article

    01/21/2010
    The CDO gene displays tissue-specific expression, with the highest mRNA level present in liver and with detectable levels found in kidney, lung, brain and small intestine.

    Murine cysteine dioxygenase gene: structural organization, tissue-specific expression and promoter identification.
    Hirschberger LL, Daval S, Stover PJ, Stipanuk MH.

    01/21/2010
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