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Specific activities of eight enzymes involved in glycerol metabolism were determined in crude extracts of three strains of Neurospora crassa after growth on six different carbon sources. One of the strains was wild type, which grew poorly on glycerol as sole carbon source; the other two were mutant strains which were efficient glycerol utilizers. A possible basis for this greater efficiency of glycerol utilization was catabolite repression of glyceraldehyde kinase by glycerol in wild type, and two-fold higher glycerate kinase activity in the mutant strains after growth on glycerol, thus apparently allowing two routes for glyceraldehyde to enter the glycolytic pathway in the mutant strains but only one in wild type. The preferential entry of glyceraldehyde to the glycolytic pathway through glycerate was suggested by the lack of glyceraldehyde kinase in all three strains after growth on one or more of the carbon sources and the generally higher levels of aldehyde dehydrogenase and of glycerate kinase than of glyceraldehyde kinase.
G D Tom, and
M Viswanath-Reddy, and
H B Howe
February 1976,
Biochimica et biophysica acta,
G D Tom, and
M Viswanath-Reddy, and
H B Howe
January 1980,
Journal of bacteriology,
G D Tom, and
M Viswanath-Reddy, and
H B Howe
June 1954,
The Journal of biological chemistry,
G D Tom, and
M Viswanath-Reddy, and
H B Howe
March 1972,
FEBS letters,
G D Tom, and
M Viswanath-Reddy, and
H B Howe
July 1962,
Biochimica et biophysica acta,
G D Tom, and
M Viswanath-Reddy, and
H B Howe
November 1973,
The Biochemical journal,
G D Tom, and
M Viswanath-Reddy, and
H B Howe
June 1972,
The Biochemical journal,
G D Tom, and
M Viswanath-Reddy, and
H B Howe
February 1968,
Biochimica et biophysica acta,
G D Tom, and
M Viswanath-Reddy, and
H B Howe
January 1974,
Zeitschrift fur allgemeine Mikrobiologie,
G D Tom, and
M Viswanath-Reddy, and
H B Howe
July 1965,
Archives of biochemistry and biophysics,
