85328-97-8Relevant academic research and scientific papers
The N-Phosphobiotin Route: a Possible New Pathway for Biotin Coenzyme
Blonski, Casimir,Belghith, Hachemi,Klaebe, Alain,Perie, Jean-Jacques
, p. 1369 - 1374 (2007/10/02)
The formation of N-acylureas from N-phosphorylated ureas under very mild conditions is presented as a possible route to the formation of carboxybiotin from biotin in biotin-mediated enzymatic carboxylations in which an N-phosphobiotin is the activated form.The detailed mechanistic pathway for the model reaction indicates that an intermediate acylphosphate is formed, the rate-determining step being a nucleophilic attack of the ureido anion or its enol on this acylphosphate.In no case was an O-phosphorylated intermediate (of the phosphobiotin type) involved.
NEW PHOSPHORYLATING AGENTS FOR GENERAL SYNTHESIS OF MIXED PHOSPHATE ESTERS
Nagamatsu, Tomohisa,Kunieda, Takehisa
, p. 2375 - 2378 (2007/10/02)
An effective procedure has been developed for the general synthesis of mixed alkyl or aryl phosphate esters by metal-catalyzed phosphorylation of alcohols with aryl bis(2-oxo-3-oxazolinyl)phosphinate.Among metallic acetylacetonates examined as catalysts, the zirconium complex was the most effective as in activity order of Zr(IV)> Ce(III)> Zn(II)> Mn(III)> Mn(II)-complexes.
MODELES DE BIOTINE ACTIVEE PAR PHOSPHORYLATION TRANSFERT DE PHOSPHORYLE
Etemad-Moghadam, G.,Blonski, C.,Gasc, M. B.,Perie, J. J.,Klaebe, A.
, p. 367 - 376 (2007/10/02)
This work describes the synthesis of the first two O-phosphobiotin models, which mimic the activated form of biotin through a phosphorylation process.In addition, pyrophosphate bond formation is considered through this kind of O-phosphorylated intermediate.Reversible interconversion of the S- and N-phosphorylated urea structures is depicted and implications of the activation process are presented.
MODELS OF BIOTIN COENZYME REACTIONS ACTIVATED THROUGH PHOSPHORYLATION
Blonski, C.,Etemad-Moghadam, G.,Gasc, M. B.,Klaebe, A.,Perie, J. J.
, p. 361 - 364 (2007/10/02)
The reactivity of models of enzymatic carboxylation reactions mediated by biotin coenzyme is presented; a possible role of the requiered ATP molecule for these reactions was investigated.Several models of biotin activated through phosphorylation - according to the O-phosphobiotin model - are described and their reactivity towards carboxylating agents discussed.Models also exhibit phosphoryl transfer propeties which may mimic known ATP synthesis from ADP, catalyzed by biotin carboxylases.Possible involvement of the same O-phosphobiotin structure is considered.
