87-51-4Relevant articles and documents
A study of the kinetics and mechanism of oxidation of L-tryptophan by diperiodatonickelate(IV) in aqueous alkaline medium
Chimatadar,Basavaraj,Nandibewoor
, p. 1046 - 1053 (2007)
The kinetics of oxidation of L-tryptophan by diperiodatonickelate(IV) (DPN) in an aqueous alkaline medium at a constant ionic strength of 0.30 mol dm -3 was studied spectrophotometrically. The reaction was first order in diperiodatonickelate(IV) and less than first order in tryptophan and the OH- ion. The addition of periodate had no effect on the reaction, and nickel(II) produced did not influence the reaction rate significantly. An increase in ionic strength and decrease in medium permittivity did not affect the reaction rate. A mechanism involving the formation of a complex between L-tryptophan and reactive DPN species was proposed. The constants characterizing the mechanism were evaluated. The activation parameters for the slow reaction step were computed and discussed.
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Sielo et al.
, p. 397,400 (1969)
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HETEROCYCLIC COMPOUND, APPLICATION THEREOF, AND COMPOSITION CONTAINING SAME
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, (2022/03/07)
A heterocyclic compound represented by formula XI, a pharmaceutically acceptable salt, a solvate, or a solvate of a pharmaceutically acceptable salt thereof, use thereof, and a composition containing the same. The compound is novel in structure and has good STAT5 inhibitory activity.
Oxidation of Primary Alcohols and Aldehydes to Carboxylic Acids via Hydrogen Atom Transfer
Tan, Wen-Yun,Lu, Yi,Zhao, Jing-Feng,Chen, Wen,Zhang, Hongbin
supporting information, p. 6648 - 6653 (2021/09/08)
The oxidation of primary alcohols and aldehydes to the corresponding carboxylic acids is a fundamental reaction in organic synthesis. In this paper, we report a new chemoselective process for the oxidation of primary alcohols and aldehydes. This metal-free reaction features a new oxidant, an easy to handle procedure, high isolated yields, and good to excellent functional group tolerance even in the presence of vulnerable secondary alcohols and tert-butanesulfinamides.
Expanding the repertoire of nitrilases with broad substrate specificity and high substrate tolerance for biocatalytic applications
Rayavarapu, Pratima,Shah, Shikha,Sunder, Avinash Vellore,Wangikar, Pramod P.
, p. 289 - 296 (2020/05/18)
Enzymatic conversion of nitriles to carboxylic acids by nitrilases has gained significance in the green synthesis of several pharmaceutical precursors and fine chemicals. Although nitrilases from several sources have been characterized, there exists a scope for identifying broad spectrum nitrilases exhibiting higher substrate tolerance and better thermostability to develop industrially relevant biocatalytic processes. Through genome mining, we have identified nine novel nitrilase sequences from bacteria and evaluated their activity on a broad spectrum of 23 industrially relevant nitrile substrates. Nitrilases from Zobellia galactanivorans, Achromobacter insolitus and Cupriavidus necator were highly active on varying classes of nitriles and applied as whole cell biocatalysts in lab scale processes. Z. galactanivorans nitrilase could convert 4-cyanopyridine to achieve yields of 1.79 M isonicotinic acid within 3 h via fed-batch substrate addition. The nitrilase from A. insolitus could hydrolyze 630 mM iminodiacetonitrile at a fast rate, effecting 86 % conversion to iminodiacetic acid within 1 h. The arylaliphatic nitrilase from C. necator catalysed enantioselective hydrolysis of 740 mM mandelonitrile to (R)-mandelic acid in 4 h. Significantly high product yields suggest that these enzymes would be promising additions to the suite of nitrilases for upscale biocatalytic application.