1123-95-1Relevant articles and documents
Biosynthesis of a thiamin antivitamin in clostridium botulinum
Cooper, Lisa E.,O'Leary, Seán E.,Begley, Tadhg P.
, p. 2215 - 2217 (2014)
Bacimethrin-derived 2′-methoxythiamin pyrophosphate inhibits microbial growth by disrupting metabolic pathways dependent on thiamin-utilizing enzymes. This study describes the discovery of the bacimethrin biosynthetic gene cluster of Clostridium botulinum A ATCC 19397 and in vitro reconstitution of bacimethrin biosynthesis from cytidine 5′-monophosphate.
Hydroxymethylation of pyrimidine mononucleotides with formaldehyde.
Alegria
, p. 317 - 324 (1967)
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Efficient synthesis of 5-hydroxymethyl pyrimidines and their nucleosides using microwave irradiation
Abdel-Rahman, Adel A.-H.,El Ashry, El Sayed H.
, p. 2043 - 2044 (2002)
Hydroxymethylation of uracil (1), cytosine (3), 5-hydroxymethyl-2′,3′-O-isopropylideneuridine (5), 5′-O-tert-butyldiphenylsilyl-2′,3′-O-isopropylideneuridine (7), 2′,3′-O-isopropylidenecytidine (9) and 2′,3′-O-isopropylidene-5′-O-tritylcytidine (11) was efficiently carried out with paraformaldehyde in alkaline medium under microwave irradiation in very high yield.
Structure of the N-glycosidase MilB in complex with hydroxymethyl CMP reveals its Arg23 specifically recognizes the substrate and controls its entry
Zhao, Gong,Wu, Geng,Zhang, Yan,Liu, Guang,Han, Tiesheng,Deng, Zixin,He, Xinyi
, p. 8115 - 8124 (2014)
5-Hydroxymethylcytosine (5hmC) is present in T-even phage and mammalian DNA as well as some nucleoside antibiotics, including mildiomycin and bacimethrin, during whose synthesis 5hmC is produced by the hydrolysis of 5-hydroxymethyl cytidine 5'-monophosphate (hmCMP) by an N-glycosidase MilB. Recently, the MilB-CMP complex structure revealed its substrate specificity for CMP over dCMP. However, hmCMP instead of CMP is the preferred substrate for MilB as supported by that its KM for CMP is ～27-fold higher than that for hmCMP. Here, we determined the crystal structures of MilB and its catalytically inactive E103A mutant in complex with hmCMP. In the structure of the complex, Phe22 and Arg23 are positioned in a cage-like active site resembling the binding pocket for the flipped 5-methylcytosine (5mC) in eukaryotic 5mC-binding proteins. Van der Waals interaction between the benzene ring of Phe22 and the pyrimidine ring of hmCMP stabilizes its binding. Remarkably, upon hmCMP binding, the guanidinium group of Arg23 was bent ～65° toward hmCMP to recognize its 5-hydroxymethyl group, inducing semi-closure of the cage-like pocket. Mutagenesis studies of Arg23 and bioinformatics analysis demonstrate that the positively charged Arg/Lys at this site is critical for the specific recognition of the 5-hydroxymethyl group of hmCMP. The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.
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Miller
, p. 752 (1955)
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TET-Like Oxidation in 5-Methylcytosine and Derivatives: A Computational and Experimental Study
Jonasson, Niko S. W.,Jan?en, Rachel,Menke, Annika,Zott, Fabian L.,Zipse, Hendrik,Daumann, Lena J.
, p. 3333 - 3340 (2021/09/25)
The epigenetic marker 5-methylcytosine (5mC) is an important factor in DNA modification and epigenetics. It can be modified through a three-step oxidation performed by ten-eleven-translocation (TET) enzymes and we have previously reported that the iron(IV)-oxo complex [Fe(O)(Py5Me2H)]2+ (1) can oxidize 5mC. Here, we report the reactivity of this iron(IV)-oxo complex towards a wider scope of methylated cytosine and uracil derivatives relevant for synthetic DNA applications, such as 1-methylcytosine (1mC), 5-methyl-iso-cytosine (5miC) and thymine (T/5mU). The observed kinetic parameters are corroborated by calculation of the C?H bond energies at the reactive sites which was found to be an efficient tool for reaction rate prediction of 1 towards methylated DNA bases. We identified oxidation products of methylated cytosine derivatives using HPLC-MS and GC-MS. Thereby, we shed light on the impact of the methyl group position and resulting C?H bond dissociation energies on reactivity towards TET-like oxidation.
