139640-11-2Relevant academic research and scientific papers
Biochemical studies of inositol: N -acetylglucosaminyltransferase involved in mycothiol biosynthesis in Corynebacterium diphtheria
Guo, Yuchuan,Wang, Lizhen,Guo, Jiatong,Gu, Guofeng,Guo, Zhongwu
, p. 3775 - 3782 (2017)
Mycothiol (MSH) is the predominant low molecular weight thiol produced by actinomycetes, and it plays a pivotal role in the bacterial detoxication process. 1L-myo-Inositol-1-phosphate (1L-Ins-1-P) α-N-acetylglucosaminyltransferase (GlcNAc-T), known as MshA, is the only glycosyltransferase involved in MSH biosynthesis. In this work, the MshA from Corynebacterium diphtheria, named as CdMshA, was expressed, purified, and studied in detail. Its enzymatic activity to transfer GlcNAc to 1L-Ins-1-P was confirmed by the isolation and rigorous characterization of its reaction product 3-phospho-1-d-myo-inositol-2-acetamido-2-deoxy-α-d-glucopyranoside. CdMshA was shown to accept only UDP-GlcNAc and 1L-Ins-1-P as its substrates among various tested glycosyl donors, such as UDP-GlcNAc, UDP-Gal, UDP-Glc, UDP-GalNAc and UDP-GlcA, and glycosyl acceptors, such as myo-inositol, 1L-Ins-1-P and 1D-Ins-1-P. The results have demonstrated the strict substrate selectivity of CdMshA. Furthermore, its reaction kinetics with UDP-GlcNAc and 1L-Ins-1-P as substrates were characterized, while site-directed mutagenesis of CdMshA disclosed that its amino acid residues N28, K81 and R157 were essential for its enzymatic activity.
The regioselective synthesis of enantiomerically pure myo-inositol derivatives. Efficient synthesis of myo-inositol 1,4,5-trisphosphate
Aguilo, Agustin,Martin-Lomas, Manuel,Penades, Soledad
, p. 401 - 404 (2007/10/02)
Regioselective 1-O-acylation of myo-inositol and simultaneous optical resolution has been achieved by perborylation, transmetallation using di-n-butyltin-bis-acetylacetonate and then acylation with (-)-menthyl chloroformate. Diastereomerically pure 1-O-(-
