Open AccessNAD(P) + Analogues: Tools for the Investigation of the Active Site of Oestradiol 17β‐Dehydrogenase from Human Placenta
Author(s) -
BIELLMANN JeanFrancois,
HIRTH Christian G.
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb02262.x
Subject(s) - nad+ kinase , substituent , chemistry , cofactor , stereochemistry , nicotinamide adenine dinucleotide , nicotinamide , nitrile , oxidoreductase , glycerol 3 phosphate dehydrogenase , amide , enzyme , biochemistry , organic chemistry
Oestradiol‐17β: NAD + 17‐oxidoreductase from human placenta can accept coenzyme analogues of NAD + and NADP + where the amide group is replaced by methyl ketone, nitrile or thioamide. The inhibition with analogues of NAD + has been studied. The presence of a substituent at C‐3 of the pyridinium ring is necessary for the binding. The inhibition by C‐4 methylated analogues is very poor, and the effect of a methyl group at C‐5 depends on the substituent at C‐3. The 1,4,5,6‐tetra‐hydronicotinamide adenine dinucleotide is a competitive inhibitor. Nicotinamide 8‐bromoadenine dinucleotide and nicotinamide 8‐thioadenine dinucleotide are efficient hydrogen acceptors.