EC Number   |
Protein Variants |
Reference |
|---|
   2.7.9.4 | C1019S |
site-directed mutagenesis, the mutant is redox-insensitiv in contrast to the wild-type enzyme |
739353 |
| 2.7.9.4 | H1004A |
lacks autophosphorylation, fails to stimulate beta-amylase 3-catalyzed starch breakdown, similar binding to starch granules as wild-type enzyme (in vitro), H1004: conserved residue within phosphohistidine domain |
676637 |
| 2.7.9.4 | H992A |
mutant enzyme backgroun level of activity, no autophosphorylation |
660961 |
| 2.7.9.4 | more |
construction of transgenic Arabidopsis thaliana plants, i.e. gwd-c1, gwd-c2, and gwd-c1/gwd-c2 or sex1-8, with reduced or no GWD activity. Absence of GWD results in altered starch granule morphology but no change in the physicochemical properties of starch granules, phenotype, overview. Partially complemented GWD transgenic lines exhibit an intermediate phenotype. Effects of the mutations on starch-related enzymes in the four Arabidopsis lines, overview |
739181 |
| 2.7.9.4 | more |
generation of antisense transgenic lines which reveal more but smaller tubers |
738013 |
| 2.7.9.4 | more |
generation of transgenic plants expressing constitutively active GWD and of Arabidopsis plants expressing a dexamethasone-inducible silencing (RNAi) construct targeted at GWD. These plants retain normal control of starch degradation in leaves. Analysis of changes in GWD protein abundance in relation to starch levels in wild-type plants, in transgenic plants in which GWD transcripts are strongly reduced by induction of RNA interference, and in transgenic plants overexpressing GWD, overview |
739353 |
| 2.7.9.4 | more |
in enzyme deficient mutant plants, phosphorylation at both C6- and C3-positions of glucose moieties in starch is dramatically decreased. In mutant plants lacking phosphoglucan, water dikinase EC 2.7.9.5, C3-bound phosphate is reduced to levels close to detection limit |
673664 |
| 2.7.9.4 | more |
production of transgenic Triticum aestivum lines using RNAi targeted to the endosperm only resulting in reduction in both GWD protein abundance and starch phosphate content |
739271 |
| 2.7.9.4 | more |
recombinant production of enzyme fragments SBD and N11 corresponding to the fragments resulting from limited proteolysis of enzyme by trypsin. Fragment N11 shows starch phosphorylating activity and a specific activity 2fold higher than that of wild-type and a doubling of Km value for potato starch substrate. N11 exhibits a higher preference for phosphorylating shorter chains compared to wild-type. Using amylose as substrate, N11 shows 5fold higher specific activity |
672151 |
| 2.7.9.4 | W117A |
mutation in tandem repeat sequence SBD-1, mutant shows extremely weak glucan binding |
672151 |
