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Literature summary for 2.4.1.18 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)

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

Protein Variants

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

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

Organism

Organism UniProt Comment Textmining
Zea mays Q08047
-
-
Zea mays CG102 Q08047
-
-

Posttranslational Modification

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

Source Tissue Comment Organism Textmining
endosperm
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Zea mays
-

Synonyms

Synonyms Comment Organism
SBEIIB
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Zea mays
starch branching enzyme IIb
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Zea mays

General Information

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