Molecular properties of the glyoxysomal and mitochondrial isoenzyme of malate dehydrogenase (EC 1.1.1.37 ; L-malate : NAD + oxidoreductase) from watermelon cotyledons (Citrullus vulgar& Schrad.) were investigated, using completely purified enzyme preparations. The apparent molecular weights of the g
Sequence homologies between glyoxysomal and mitochondrial malate dehydrogenase
β Scribed by C. Gietl; F. Lottspeich; B. Hock
- Publisher
- Springer-Verlag
- Year
- 1986
- Tongue
- English
- Weight
- 509 KB
- Volume
- 169
- Category
- Article
- ISSN
- 0032-0935
No coin nor oath required. For personal study only.
β¦ Synopsis
The comparison of mitochondrial and glyoxysomal malate dehydrogenase (EC 1.1.1.37) from cotyledons of germinating watermelon (Citrullus vulgaris Schrad., cv. Kleckey's Sweet No. 6) by means of serological methods and peptide patterns revealed a high degree of homology. The Nterminal sequence analysis yielded a distinct presequence of eight or nine amino-acid residues, respectively, which is followed by an almost identical stretch of at least 20 amino-acid residues. A very similar domain has been recognized for mitochondrial malate dehydrogenase from porcine heart and yeast, and for Eseherichia coli malate dehydrogenase.
π SIMILAR VOLUMES
Kinetic parameters of the glyoxysomal and mitochondrial malate dehydrogenase (EC 1.1.1.37) of watermelon (Citrullus vulgaris Schrad.) cotyledons were compared. The data were obtained by initial rate experiments at pH 8.5 in both directions of the reaction using homogeneous enzyme preparations. Subst
In order to investigate a possible association between soybean malate synthase (MS; L-malate glyoxylate-lyase, CoA-acetylating, EC 4.1.3.2) and glyoxysomal malate dehydrogenase (gMDH; (S)-malate: NAD Β§ oxidoreductase, EC 1.1.1.37), two consecutive enzymes in the glyoxylate cycle, their elution profi