Literature DB >> 214386

Studies on the biosynthesis of cyclitols, XXXVII. On mechanism and function of Schiff's base formation as an intermediary reaction step of myo-inositol-1-phosphate synthase from rat testicles.

F Pittner, O Hoffmann-Ostenhof.   

Abstract

It could be shown that the formation of a Schiff's base by myo-inositol-1-phosphate synthase of rat testicles occurs by binding the aldehyde group of the open form of its substrate, D-glucose 6-phosphate, to a lysyl residue of one or both smaller subunits of the enzyme. The participation of the Schiff's base formation in the catalytic process is supported by the observations that (a) no Schiff's base is formed if NAD is removed from the enzyme, and (b) in the presence of NAD, the dehydrogenation step involved in the catalytic mechanism apparently takes place rapidly after the formation of the Schiff's base.

Entities:  

Mesh:

Substances:

Year:  1978        PMID: 214386     DOI: 10.1515/bchm2.1978.359.2.1395

Source DB:  PubMed          Journal:  Hoppe Seylers Z Physiol Chem        ISSN: 0018-4888


  3 in total

1.  Immobilization ofmyo-inositol-1-phosphate synthase containing active, self-regenerating coenzyme (NAD(+)) on the same matrix.

Authors:  F Pittner
Journal:  Appl Biochem Biotechnol       Date:  1981-06       Impact factor: 2.926

2.  Preparation of homogeneous crystals of myo-inositol 1-phosphate synthase from rat testicles--further data on the chemical and catalytic properties of the enzyme (studies on the biosynthesis cyclitols, XXXIX).

Authors:  F Pittner; O Hoffmann-Ostenhof
Journal:  Mol Cell Biochem       Date:  1979-12-14       Impact factor: 3.396

3.  Myo-inositol-1-phosphate synthase from streptomyces griseus (studies on the biosynthesis of cyclitols, XXXVIII).

Authors:  F Pittner; I I Tovarova; E Y Kornitskaya; A S Khokhlov; O Hoffmann-Ostenhof
Journal:  Mol Cell Biochem       Date:  1979-05-06       Impact factor: 3.396

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.