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Literature summary extracted from

  • Makhmoudova, A.; Williams, D.; Brewer, D.; Massey, S.; Patterson, J.; Silva, A.; Vassall, K.A.; Liu, F.; Subedi, S.; Harauz, G.; Siu, K.W.; Tetlow, I.J.; Emes, M.J.
    Identification of multiple phosphorylation sites on maize endosperm starch branching enzyme IIb, a key enzyme in amylopectin biosynthesis (2014), J. Biol. Chem., 289, 9233-9246.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.18 recombinant expression of wild-type and mutant enzymes Zea mays

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.18 additional information generation of N- and C-terminally truncated enzyme mutants. Activities of kinases on wild-type and enzyme mutants, overview Zea mays
2.4.1.18 S147A site-directed mutagenesis Zea mays
2.4.1.18 S204A site-directed mutagenesis Zea mays
2.4.1.18 S286A site-directed mutagenesis Zea mays
2.4.1.18 S286A/S297A/S649A site-directed mutagenesis Zea mays
2.4.1.18 S297A site-directed mutagenesis Zea mays
2.4.1.18 S297A/S298A site-directed mutagenesis Zea mays
2.4.1.18 S298A site-directed mutagenesis Zea mays
2.4.1.18 S568A site-directed mutagenesis Zea mays
2.4.1.18 S598A site-directed mutagenesis Zea mays
2.4.1.18 S649A site-directed mutagenesis Zea mays
2.4.1.18 S659A site-directed mutagenesis Zea mays
2.4.1.18 S699A site-directed mutagenesis Zea mays
2.4.1.18 S705A site-directed mutagenesis Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.18 amyloplast developing Zea mays 9501
-

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Zea mays Q08047
-
-
2.4.1.18 Zea mays CG102 Q08047
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.18 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

EC Number Source Tissue Comment Organism Textmining
2.4.1.18 endosperm
-
Zea mays
-

Synonyms

EC Number Synonyms Comment Organism
2.4.1.18 SBEIIB
-
Zea mays
2.4.1.18 starch branching enzyme IIb
-
Zea mays

General Information

EC Number General Information Comment Organism
2.4.1.18 additional information molecular dynamics simulation and modeling of phosphorylation of enzyme mutants Zea mays
2.4.1.18 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