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Studies on regulatory functions of malic enzymes. V. Comparative studies of malic enzymes in bacteria.
- Source :
-
Journal of biochemistry [J Biochem] 1978 May; Vol. 83 (5), pp. 1387-94. - Publication Year :
- 1978
-
Abstract
- Screening of four malic enzymes--NAD-linked enzyme [EC 1.1.1.38], NAD, NADP-linked enzyme [EC 1.1.1.39], NADP-linked enzyme [EC 1.1.1.40], and D-malic enzyme--was carried out with cell-free extracts of the following 16 strains of bacteria by the aid of Sepharose 6B column chromatography: 9 strains of enteric bacteria, 3 strains of Pseudomonas, Alcaligenes faecalis, Agrobacterium tumefaciens, Rhodospirillum rubrum, and Clostridium tetanomorphum. All the strains tested contained at least one malic enzyme. The NADP-linked enzyme activity was found in all the strains except C. tetanomorphum, the NAD-linked enzyme activity in 12 strains--8 strains of enteric bacteria, 2 strains of Pseudomonas, Ag. tumefaciens, and C. tetanomorphum--and D-malic enzyme activity in 4 strains--A, aerogenes (IFO 3319 and 12059), Ps. fluorescens, and R. rubrum. The NADP-linked and NAD-linked enzyme activities of two strains of Pseudomonas were not separated by the chromatography. The available evidence suggested that the NAD, NADP-linked enzyme was not present in these 16 strains. The comparative studies of molecular, enzymatic, and serological properties of the malic enzymes in these 16 strains revealed a close similarity of the same types of malic enzymes among enteric bacteria.
- Subjects :
- Alcaligenes enzymology
Clostridium enzymology
Escherichia coli enzymology
Malate Dehydrogenase immunology
Malate Dehydrogenase isolation & purification
Molecular Weight
Pseudomonas enzymology
Rhizobium enzymology
Rhodospirillum rubrum enzymology
Species Specificity
Bacteria enzymology
Malate Dehydrogenase physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0021-924X
- Volume :
- 83
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 96110
- Full Text :
- https://doi.org/10.1093/oxfordjournals.jbchem.a132048