2663-91-4Relevant articles and documents
Micro-reaction system and method for continuously preparing 2-amino-1,3-diol compounds
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Paragraph 0042-0043, (2021/08/06)
The invention belongs to the technical field of pharmaceutical engineering, and particularly relates to a micro-reaction system and method for continuously preparing 2-amino-1,3-diol compounds. The micro-reaction system comprises a micro-mixer and a micro-channel reactor which communicate with each other in sequence; the micro-mixer is used for mixing a solution of a raw material 2-nitro-1,3-diol compound with hydrogen; and the micro-channel reactor is used for continuous reaction of the mixture. The method comprises the following steps: packing a palladium catalyst in the microchannel reactor, dissolving a 2-nitro-1,3-diol compound in an organic solvent, conveying the dissolved 2-nitro-1,3-diol compound and hydrogen into the microchannel reactor at the same time, and carrying out a continuous catalytic hydrogenation reaction to obtain the corresponding 2-amino-1, 3-diol compound. According to the method, the reaction time is only several minutes, the yield of the product 2-amino-1,3-diol compound is larger than 99%, the technological process is continuous, the automation degree is high, the space time yield is high, operation is easy and convenient, the step of separating reaction liquid from a catalyst is not needed, cost is low, and the method is environmentally friendly, safe and easy for industrial production.
CmlI is an N-oxygenase in the biosynthesis of chloramphenicol
Lu, Haige,Chanco, Emmanuel,Zhao, Huimin
supporting information; experimental part, p. 7651 - 7654 (2012/09/08)
The N-oxygenation of an amine group is one of the steps in the biosynthesis of the antibiotic chloramphenicol. The non-heme di-iron enzyme CmlI was identified as the enzyme catalyzing this reaction through bioinformatics studies and reconstitution of enzymatic activity. In vitro reconstitution was achieved using phenazine methosulfate and NADH as electron mediators, while in vivo activity was demonstrated in Escherichia coli using two substrates. Kinetic analysis showed a biphasic behavior of the enzyme. Oxidized hydroxylamine and nitroso compounds in the reaction were detected both in vitro and in vivo based on LC-MS. The active site metal was confirmed to be iron based on a ferrozine assay. These findings provide new insights into the biosynthesis of chloramphenicol and could lead to further development of CmlI as a useful biocatalyst.
Correlation between antigen-combining-site structures and functions within a panel of catalytic antibodies generated against a single transition state analog
Fujii, Ikuo,Tanaka, Fujie,Miyashita, Hideaki,Tanimura, Ryuji,Kinoshita, Keiko
, p. 6199 - 6209 (2007/10/02)
The diversity of the immune response, which can provide a panel of catalytic antibodies with varying degrees of catalytic activity and substrate specificity by immunization with a single hapten, raises the question concerning the extent to which a rationa