EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Reference |
---|
1.1.1.363 | -999 |
- |
a method is described which enables one to assay simultaneously the NAD+- and NADP+-linked reactions of dehydrogenases which can utilize both coenzymes. The method is based on the fact that the thionicotinamide analogs of NADH and NADPH absorb light maximally at 400 nm, a wavelength sufficiently far removed from the absorbance maximum of NADH and NADPH to permit measurements of the simultaneous reduction of NAD+ (or NADP+) and the thionicotinamide analog of NADP+ (or NAD+). Application of the method to glucosed 6-phosphate dehydrogenase from Leuconostoc mesenteroides reveals differential effects of glucose 6-phosphate concentration on the NAD+- and NADP+-linked reactions catalyzed by this enzyme which can not be detected by conventional assay procedures and which may have regulatory significance |
722581 |
1.1.1.363 | -999 |
- |
the His-tagged form of PputG6PDH-1 shows no significant differences with respect to the non-tagged form of the same enzyme |
742533 |
1.1.1.363 | 0.006 |
- |
enzyme in Pseudomonas putida KT2440 crude cell extract, pH 8.0, 30°C, with NADP+ |
742533 |
1.1.1.363 | 0.006 |
- |
with NADP+ as cofactor, at pH 8.0 and 30°C |
740461 |
1.1.1.363 | 0.008 |
- |
recombinant enzyme in Escherichia coli MG1655 crude cell extract, pH 8.0, 30°C, with NAD+ |
742533 |
1.1.1.363 | 0.025 |
- |
enzyme in Pseudomonas putida KT2440 crude cell extract, pH 8.0, 30°C, with NAD+ |
742533 |
1.1.1.363 | 0.025 |
- |
with NAD+ as cofactor, at pH 8.0 and 30°C |
740461 |
1.1.1.363 | 0.103 |
- |
recombinant enzyme in Escherichia coli MG1655 crude cell extract, pH 8.0, 30°C, with NADP+ |
742533 |
1.1.1.363 | 145.7 |
- |
pH 8.0, 30°C, NADP+ |
762314 |
1.1.1.363 | 715 |
- |
25°C, pH 7.6, wild-type enzyme |
723718 |