Nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in wheat endosperm at serine-404 by an SNF1-related protein kinase allosterically inhibited by ribose-5-phosphate. [electronic resource]
Producer: 20111025Description: 1337-50 p. digitalISSN:- 1532-2548
- Allosteric Regulation -- drug effects
- Amino Acid Sequence
- Cations, Divalent -- pharmacology
- Endosperm -- drug effects
- Fructosediphosphates -- pharmacology
- Glyceraldehyde-3-Phosphate Dehydrogenases -- metabolism
- Glyceric Acids -- pharmacology
- Kinetics
- Models, Biological
- Molecular Sequence Data
- Organ Specificity -- drug effects
- Peptides -- metabolism
- Phosphorylation -- drug effects
- Phosphoserine -- metabolism
- Protein Serine-Threonine Kinases -- antagonists & inhibitors
- Ribosemonophosphates -- pharmacology
- Sequence Alignment
- Triticum -- drug effects
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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