Premium
Inhibition of the conversion of glycine to serine in spinach leaf mitochondria
Author(s) -
Gardeström Per,
Bergman Anders,
Ericson Ingemar
Publication year - 1981
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1981.tb02728.x
Subject(s) - serine hydroxymethyltransferase , glycine , serine , chemistry , non competitive inhibition , bicarbonate , spinacia , biochemistry , amino acid , enzyme , organic chemistry , chloroplast , gene
Isonicotinyl hydrazide, glycine hydroxamate, aminoacetonitrile and KCN inhibited the conversion of glycine to serine in spinach ( Spinacea oleracea L. cv. Viking II) mitochondria. The site of inhibition for the different inhibitors was studied. Isonicotinyl hydrazide and glycine hydroxamate both inhibited the partial reactions glycine‐bicarbonate exchange and serine hydroxymethyltransferase. The inhibition was competitive for the exchange reaction and noncompetitive for serine hydroxymethyltransferase. Aminoacetonitrile at low concentration (1 m M ) inhibited the glycine‐bicarbonate exchange specifically, whereas serine hydroxymethyltransferase was inhibited only at higher concentrations. Aminoacetonitrile was a competitive inhibitor for both reactions. The serine hydroxymethyltransferase was inhibited by KCN whereas the glycine‐bicarbonate exchange was only partially inhibited. The KCN‐inhibition of serine hydroxymethyltransferase was competitive.