Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes | Zea mays |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of N- and C-terminally truncated enzyme mutants. Activities of kinases on wild-type and enzyme mutants, overview | Zea mays |
S147A | site-directed mutagenesis | Zea mays |
S204A | site-directed mutagenesis | Zea mays |
S286A | site-directed mutagenesis | Zea mays |
S286A/S297A/S649A | site-directed mutagenesis | Zea mays |
S297A | site-directed mutagenesis | Zea mays |
S297A/S298A | site-directed mutagenesis | Zea mays |
S298A | site-directed mutagenesis | Zea mays |
S568A | site-directed mutagenesis | Zea mays |
S598A | site-directed mutagenesis | Zea mays |
S649A | site-directed mutagenesis | Zea mays |
S659A | site-directed mutagenesis | Zea mays |
S699A | site-directed mutagenesis | Zea mays |
S705A | site-directed mutagenesis | Zea mays |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
amyloplast | developing | Zea mays | 9501 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | Q08047 | - |
- |
Zea mays CG102 | Q08047 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | native and recombinant maize SBEIIb are used as substrates for amyloplast protein kinases to identify phosphorylation sites on the protein, bioinformatics, site-directed mutagenesis, and mass spectrometry identify three phosphorylation sites at Ser residues: Ser649, Ser286, and Ser297. Ca2+-dependent protein kinases from amyloplasts, termed K1, responsible for Ser649 and Ser286 phosphorylation, and K2, responsible for Ser649 and Ser297 phosphorylation. The Ser286 and Ser297 phosphorylation sites are conserved in all plant branching enzymes and are located at opposite openings of the 8-stranded parallel beta-barrel of the active site, which is involved with substrate binding and catalysis. Molecular dynamics simulation analysis indicates that phospho-Ser297 forms a stable salt bridge with Arg665, part of a conserved Cys-containing domain in plant branching enzymes. Ser649 conservation appears confined to the enzyme in cereals and is not universal, and is presumably associated with functions specific to seed storage | Zea mays |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
endosperm | - |
Zea mays | - |
Synonyms | Comment | Organism |
---|---|---|
SBEIIB | - |
Zea mays |
starch branching enzyme IIb | - |
Zea mays |
General Information | Comment | Organism |
---|---|---|
additional information | molecular dynamics simulation and modeling of phosphorylation of enzyme mutants | Zea mays |
physiological function | starch branching enzyme IIb plays a crucial role in amylopectin biosynthesis in maize endosperm by defining the structural and functional properties of storage starch and is regulated by protein phosphorylation | Zea mays |