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[ CAS No. 2038-57-5 ] {[proInfo.proName]}

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Chemical Structure| 2038-57-5
Chemical Structure| 2038-57-5
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Anushree Mondal ; Pronay Roy ; Jaclyn Carrannatto , et al. DOI: PubMed ID:

Abstract: The prenylated-flavin mononucleotide-dependent decarboxylases (also known as UbiD-like enzymes) are the most recently discovered family of decarboxylases. The modified flavin facilitates the decarboxylation of unsaturated carboxylic acids through a novel mechanism involving 1,3-dipolar cyclo-addition chemistry. UbiD-like enzymes have attracted considerable interest for biocatalysis applications due to their ability to catalyse (de)carboxylation reactions on a broad range of aromatic substrates at otherwise unreactive carbon centres. There are now ～35[thin space (1/6-em)]000 protein sequences annotated as hypothetical UbiD-like enzymes. Sequence similarity network analyses of the UbiD protein family suggests that there are likely dozens of distinct decarboxylase enzymes represented within this family. Furthermore, many of the enzymes so far characterized can decarboxylate a broad range of substrates. Here we describe a strategy to identify potential substrates of UbiD-like enzymes based on detecting enzyme-catalysed solvent deuterium exchange into potential substrates. Using ferulic acid decarboxylase (FDC) as a model system, we tested a diverse range of aromatic and heterocyclic molecules for their ability to undergo enzyme-catalysed H/D exchange in deuterated buffer. We found that FDC catalyses H/D exchange, albeit at generally very low levels, into a wide range of small, aromatic molecules that have little resemblance to its physiological substrate. In contrast, the sub-set of aromatic carboxylic acids that are substrates for FDC-catalysed decarboxylation is much smaller. We discuss the implications of these findings for screening uncharacterized UbiD-like enzymes for novel (de)carboxylase activity.

Purchased from AmBeed: ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ; ;

Zhou, Jujun ; Deng, Youchao ; Iyamu, Iredia D. , et al. DOI: PubMed ID:

Abstract: S-Adenosyl-L-methionine (SAM) analogs are adaptable tools for studying and therapeutically inhibiting SAM-dependent methyltransferases (MTases). Some MTases play significant roles in host-pathogen interactions, one of which is Clostridioides difficile-specific DNA adenine MTase (CamA). CamA is needed for efficient sporulation and alters persistence in the colon. To discover potent and selective CamA inhibitors, we explored modifications of the solvent-exposed edge of the SAM adenosine moiety. Starting from the two parental compounds (6e and 7), we designed an adenosine analog (11a) carrying a 3-phenylpropyl moiety at the adenine N6-amino group, and a 3-(cyclohexylmethyl guanidine)-Et moiety at the sulfur atom off the ribose ring. Compound 11a (IC50 = 0.15 μM) is 10x and 5x more potent against CamA than 6e and 7, resp. The structure of the CamA-DNA-inhibitor complex revealed that 11a adopts a U-shaped conformation, with the two branches folded toward each other, and the aliphatic and aromatic rings at the two ends interacting with one another. 11a occupies the entire hydrophobic surface (apparently unique to CamA) next to the adenosine binding site. Our work presents a hybrid knowledge-based and fragment-based approach to generating CamA inhibitors that would be chem. agents to examine the mechanism(s) of action and therapeutic potentials of CamA in C. difficile infection.

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Product Details of [ 2038-57-5 ]

CAS No. :2038-57-5 MDL No. :MFCD00008224
Formula : C9H13N Boiling Point : -
Linear Structure Formula :- InChI Key :LYUQWQRTDLVQGA-UHFFFAOYSA-N
M.W : 135.21 Pubchem ID :16259
Synonyms :

Safety of [ 2038-57-5 ]

Signal Word:Danger Class:8
Precautionary Statements:P210-P264-P280-P301+P330+P331-P303+P361+P353-P304+P340+P310-P305+P351+P338+P310-P363-P370+P378-P403+P235-P405-P501 UN#:2735
Hazard Statements:H227-H314 Packing Group:Ⅲ
GHS Pictogram:

Application In Synthesis of [ 2038-57-5 ]

* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.

  • Downstream synthetic route of [ 2038-57-5 ]

[ 2038-57-5 ] Synthesis Path-Downstream   1~3

  • 1
  • [ 1194-21-4 ]
  • [ 2038-57-5 ]
  • [ 98510-50-0 ]
  • 2
  • [ 2038-57-5 ]
  • [ 4023-02-3 ]
  • [ 1458-01-1 ]
  • <i>N</i>-(3,5-diamino-6-chloro-pyrazine-2-carbonyl)-<i>N</i>'-(3-phenyl-propyl)-guanidine [ No CAS ]
  • 3
  • [ 6624-49-3 ]
  • [ 2038-57-5 ]
  • [ 1354716-31-6 ]
YieldReaction ConditionsOperation in experiment
With benzotriazol-1-ol; diisopropyl-carbodiimide; In dichloromethane; at 20℃; General procedure: One milli mole of the carboxylic acid was dissolved in DCM. To this, 1.1 equiv of HOBt and the desired primary amine were added. Following this, 1 equiv of DIC was added to the mixture and the reaction was mixed overnight. Upon completion of the reaction, the diisopropylurea was filtered away and the DCM layer was washed with saturated bicarbonate solution (1.x.) and 2 M HCl (1.x.). The organic layer was dried over anhydrous sodium sulfate and the solvent was then removed under reduced pressure. Typical yields for all amide bond formations were 80percent. A small portion of the resulting compounds were carried through and used for HPLC purification.
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