Open AccessOn the Conformation of Pyridoxal Phosphate Imine in Solution and in Aspartate‐Aminotransferase Active Site
Author(s) -
TUMANYAN Vladymir G.,
MAMAEVA Olga K.,
BOCHAROV Alexander L.,
IVANOV Valery I.,
KARPEISKY Marat Y.,
YAKOVLEV Gennady I.
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03879.x
Subject(s) - imine , pyridoxal , chemistry , pyridoxal phosphate , steric effects , active site , ring (chemistry) , stereochemistry , oxime , crystallography , enzyme , medicinal chemistry , organic chemistry , cofactor , catalysis
The work comprises:1 Determination by nuclear magnetic resonance method of the conformation of the imino group of pyridoxal‐ P oxime in solution. It has been found to be nearly coplanar with the aromatic ring. 2 Theoretical calculation by the method of atom‐atom potentials of the permitted conformations of pyridoxal‐ P imine and its analogs: 6‐methylpyridoxal‐ P and 5′‐methylpyridoxal‐ P . There have been found seven favourable conformations for pyridoxal‐ P imine, some of which were prohibited in the analogs mentioned. 3 Experimental estimation of the conformation of pyridoxal‐ P imine in the active site of aspartate aminotransferase with the use of the above sterically hindered analogs and 5′‐deoxy‐5′‐carboxy‐methylenepyridoxal analog. In result, the number of the possible conformations for pyridoxal‐ P imine in the active site has been reduced to a pair of symmetrical conformations.