EC Number   |
Activating Compound |
Reference  |
|---|
    1.1.1.82 | dithiothreitol |
activates |
286653, 287384, 287392, 287393, 287410 |
| 1.1.1.82 | more |
activation by light |
287384, 287391, 287395, 287398, 287399, 287412, 287414, 287419, 287425 |
| 1.1.1.82 | more |
in the absence of photosynthetic electron flow, the chloroplast enzyme exists in its disulfide-containing form which is inactive under physiological conditions. Upon interaction with reduced thioredoxin generated in the light, the active dithiol-containing enzyme is formed |
287389 |
| 1.1.1.82 | acetone |
increases the activity of the oxidized truncated enzyme form, optimal concentration 15% |
287392 |
| 1.1.1.82 | carboxypeptidase Y |
incubation of the native oxidized enzyme at pH 6.0, 25°C, results in slow activation. A small carboxy-terminal peptide of the native enzyme is accessible to proteolytic degradation followed by activation of the inactive oxidized enzyme. This peptide is involved in the regulation of activity, tetramer formation and thioredoxin binding |
287392 |
| 1.1.1.82 | methanol |
increases the activity of the oxidized truncated enzyme form, optimal concentration 8% |
287392 |
| 1.1.1.82 | more |
activation by light results from the thioredoxin-mediated reduction of two disulfides, located, respectively, in N- and C-terminal sequence extensions typical of all NADP-dependent light-regulated enzyme forms. The activation is a result of the unobstruction of the active site by acquisition of an additional mobility of the C-terminal 15-residue stretch |
287395 |
| 1.1.1.82 | thioredoxin |
strong activation |
287397 |
| 1.1.1.82 | more |
3,4-dichlorophenyl-1,1-dimethylurea, up to 0.033 mM, strongly inhibits light activation |
287398 |
| 1.1.1.82 | more |
noncyclic electron flow is required for activation of the enzyme |
287398 |
