Works (6)

Updated: July 5th, 2023 16:04

2000 review

Carbon and nitrogen metabolism and reversible protein phosphorylation

[Review of ]. ADVANCES IN BOTANICAL RESEARCH INCORPORATING ADVANCES IN PLANT PATHOLOGY, VOL 32, 32, 435–458.

By: D. Toroser* & S. Huber*

TL;DR: This chapter focuses on the regulation of activity of several enzymes involved in carbon- and nitrogen-metabolisms that are phosphorylated by either calmodulin-like domain protein kinases (CDPKs) or sucrose nonfermenting-1 (SNF1)-related protein. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2000 journal article

Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate

PLANT PHYSIOLOGY, 123(1), 403–411.

By: D. Toroser n, Z. Plaut & S. Huber n

MeSH headings : Barium / metabolism; Glucose-6-Phosphate / pharmacology; Hydrogen-Ion Concentration; Magnesium / metabolism; Plants / enzymology; Protein Serine-Threonine Kinases / antagonists & inhibitors; Protein Serine-Threonine Kinases / isolation & purification; Protein Serine-Threonine Kinases / metabolism; Substrate Specificity
TL;DR: Glc-6-P inhibition of PK(III) activity potentially provides a mechanism for metabolic regulation of the reactions catalyzed by these important protein kinases. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

1999 journal article

Site-directed mutagenesis of serine 158 demonstrates its role in spinach leaf sucrose-phosphate synthase modulation

PLANT JOURNAL, 17(4), 407–413.

By: D. Toroser n, R. McMichael n, K. Krause, J. Kurreck*, U. Sonnewald*, M. Stitt*, S. Huber n

MeSH headings : Base Sequence; Circadian Rhythm; DNA Primers; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Plant; Glucosyltransferases / genetics; Glucosyltransferases / metabolism; Mutagenesis, Site-Directed; Plant Leaves / enzymology; Plants, Genetically Modified / genetics; Plants, Genetically Modified / physiology; Plants, Toxic; Serine / genetics; Serine / metabolism; Spinacia oleracea / enzymology; Spinacia oleracea / genetics; Tobacco / genetics; Tobacco / physiology
TL;DR: The results demonstrate the regulatory significance of Ser158 as the major site responsible for dark inactivation of spinach SPS in vivo, and indicate that the significance of phosphorylation is the introduction of a negative charge at the Ser158 position. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

1998 journal article

3-hydroxy-3-methylglutaryl-coenzyme a reductase kinase and sucrose-phosphate synthase kinase activities in cauliflower florets: Ca2+ dependence and substrate specificities

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 355(2), 291–300.

By: D. Toroser n & S. Huber n

author keywords: protein kinase; 3-hydroxy-3-methylglutaryl-CoA reductase; Brassica oleracea; sucrose-phosphate synthase; phosphorylation motif
MeSH headings : AMP-Activated Protein Kinases; Amino Acid Sequence; Binding Sites; Brassica; Calcium / physiology; Chromatography, Gel; Enzyme Activation; Glucosyltransferases / isolation & purification; Glucosyltransferases / metabolism; Hydroxymethylglutaryl CoA Reductases / metabolism; Molecular Sequence Data; Molecular Weight; Multienzyme Complexes / isolation & purification; Multienzyme Complexes / metabolism; Nitrate Reductase; Nitrate Reductase (NADH); Nitrate Reductases / metabolism; Peptides / chemical synthesis; Peptides / metabolism; Phosphorylation; Plant Structures / enzymology; Protein Kinases / isolation & purification; Protein Kinases / metabolism; Protein Serine-Threonine Kinases; Spinacia oleracea; Substrate Specificity
TL;DR: The novel aspects are that PKIII has not been detected in previous cauliflower studies, that SAMS* is a more specific peptide substrate to identify potential HMGR kinases, and that the major HM GR kinase in cauliflower is Ca2+ dependent. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

1998 journal article

Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins

FEBS LETTERS, 435(1), 110–114.

By: D. Toroser n, G. Athwal n & S. Huber n

author keywords: sucrose-phosphate synthase; 14-3-3 protein; Spinach; protein : protein interaction; surface plasmon resonance
MeSH headings : 14-3-3 Proteins; Amino Acid Sequence; Aminoimidazole Carboxamide / analogs & derivatives; Aminoimidazole Carboxamide / pharmacology; Binding Sites; Enzyme Activation / drug effects; Enzyme Inhibitors / metabolism; Enzyme Inhibitors / pharmacology; Glucosyltransferases / drug effects; Glucosyltransferases / metabolism; Magnesium / metabolism; Molecular Sequence Data; Peptide Fragments / metabolism; Phosphorylation; Plant Leaves / drug effects; Plant Leaves / enzymology; Proteins / metabolism; Proteins / pharmacology; Ribonucleotides / pharmacology; Serine / metabolism; Spinacia oleracea / drug effects; Spinacia oleracea / enzymology; Tyrosine 3-Monooxygenase
TL;DR: An Mg2+‐dependent interaction between spinach leaf sucrose‐phosphate synthase (SPS) and endogenous 14‐3‐3 proteins is reported, as evidenced by co‐elution during gel filtration and co‐immunoprecipitation. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

1997 journal article

Protein phosphorylation as a mechanism for osmotic-stress activation of sucrose-phosphate synthase in spinach leaves

PLANT PHYSIOLOGY, 114(3), 947–955.

By: D. Toroser n & S. Huber n

MeSH headings : Amino Acid Sequence; Calcium / pharmacology; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Conserved Sequence; Darkness; Enzyme Activation; Glucosyltransferases / biosynthesis; Glucosyltransferases / isolation & purification; Glucosyltransferases / metabolism; Light; Molecular Sequence Data; Osmolar Concentration; Peptide Fragments / chemistry; Peptide Fragments / metabolism; Phosphopeptides / chemistry; Phosphorylation; Phosphoserine; Plant Leaves; Protein Kinases / isolation & purification; Protein Kinases / metabolism; Sequence Alignment; Spinacia oleracea / enzymology; Spinacia oleracea / physiology
TL;DR: At least part of the osmotic stress activation of SPS in dark leaves results from phosphorylation of serine-424 catalyzed by a Ca2+-dependent, 150-kD protein kinase. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

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