Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Chen, Y.B.; Lu, T.C.; Wang, H.X.; Shen, J.; Bu, T.T.; Chao, Q.; Gao, Z.F.; Zhu, X.G.; Wang, Y.F.; Wang, B.C.
    Posttranslational modification of maize chloroplast pyruvate orthophosphate dikinase reveals the precise regulatory mechanism of its enzymatic activity (2014), Plant Physiol., 165, 534-549.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.27 recombinant overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) RIL Zea mays
2.7.9.1 gene C4ppdkZm1, quantitative real-time PCR enzyme expression analysis, recombinant expression of tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (RIL) Zea mays
2.7.9.1 gene CyppdkZm2, quantitative real-time PCR enzyme expression analysis Zea mays
2.7.11.32 recombinant expression of His-tagged enzyme in Escherichia coli Zea mays

Protein Variants

EC Number Protein Variants Comment Organism
2.7.4.27 G525A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.4.27 G525P site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.4.27 H529A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.4.27 S506A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.4.27 S528A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.4.27 S528C site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.4.27 S528D site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.4.27 S528T site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.4.27 S528Y site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.4.27 T309A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.4.27 T527A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.4.27 T527D site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
2.7.9.1 G525A site-directed mutagenesis, the mutant shows no phosphorylation signal Zea mays
2.7.9.1 G525P site-directed mutagenesis, the mutant shows no phosphorylation signal Zea mays
2.7.9.1 H529A site-directed mutagenesis Zea mays
2.7.9.1 S506A site-directed mutagenesis Zea mays
2.7.9.1 S528A site-directed mutagenesis Zea mays
2.7.9.1 S528C site-directed mutagenesis, the mutant shows a phosphorylation signal only slightly weaker than the wild-type enzyme due to the tighter binding of S528 to G525 compared to C528 Zea mays
2.7.9.1 S528D site-directed mutagenesis Zea mays
2.7.9.1 S528T site-directed mutagenesis, the mutant shows no phosphorylation signal Zea mays
2.7.9.1 S528Y site-directed mutagenesis, the mutant shows no phosphorylation signal Zea mays
2.7.9.1 T309A site-directed mutagenesis Zea mays
2.7.9.1 T527A site-directed mutagenesis Zea mays
2.7.9.1 T527D site-directed mutagenesis Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.4.27 chloroplast the enzyme contains a transit peptide cleavage site Zea mays 9507
-
2.7.9.1 chloroplast high levels of PPDK protein accumulate in mesophyll chloroplasts, identification of a transit peptide cleavage site, the mature isozyme C4PPDK contains the specific N-terminal sequence TTKK Zea mays 9507
-
2.7.9.1 cytosol the mature isozyme CyPPDKZm1 contains the 11-residue sequence MAPAPCGRSSQ Zea mays 5829
-
2.7.9.1 soluble
-
 Zea mays
-
-
2.7.11.32 chloroplast
-
 Zea mays 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.9.1 Mg2+ required Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.27 [pyruvate, phosphate dikinase] phosphate + phosphate Zea mays
-
 [pyruvate, phosphate dikinase] + diphosphate reversible phosphorylation at Thr527 by maize pyruvate orthophosphate dikinase regulatory protein. The level of C4PPDK phosphorylated at Ser528 is much lower than that at Thr527 in maize leaves, meaning that phosphorylation at Ser528 is not as important as at Thr527 for the regulation of PPDK activity. The bifunctional enzyme exhibits kinase activity, EC 2.7.11.32, and dephosphorylation activity, EC 2.7.4.27 ?
2.7.9.1 ATP + pyruvate + phosphate Zea mays
-
 AMP + phosphoenolpyruvate + diphosphate
-
 r
2.7.11.32 ADP + [pyruvate, phosphate dikinase] Zea mays reversible phosphorylation at Thr527 and Ser528, but not Thr309 and Ser506, of PPDK AMP + [pyruvate, phosphate dikinase] phosphate
-
 r
2.7.11.32 additional information Zea mays PPDK regulatory protein (PDRP) is a unique bifunctional enzyme, catalyzes this light-dependent regulation by reversible phosphorylation of an active-site Thr527 in PPDK ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.27 Zea mays Q195N6 isozyme C4 chloroplast PPDK, i.e. C4ppdk, gene PDRP1
-
2.7.9.1 Zea mays P11155 ecotype B73
-
2.7.9.1 Zea mays Q42368 ecotype B73
-
2.7.11.32 Zea mays
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.4.27 proteolytic modification the enzyme contains a transit peptide cleavage site Zea mays
2.7.4.27 side-chain modification N-terminal acetylation of nucleus-encoded chloroplast proteins in the cytosol, e.g. of isozyme C4 chloroplast PPDK, is required for proper chloroplast characteristics, such as the stability and/or import competence of organellar precursor proteins Zea mays
2.7.9.1 additional information partial amino-terminal acetylation of the plastidic isozyme Zea mays
2.7.9.1 phosphoprotein in C4 plants, pyruvate orthophosphate dikinase (PPDK) activity is tightly dark/light regulated by reversible phosphorylation of an active-site Thr residue, catalyzed by PPDK regulatory protein (PDRP). Phosphorylation and dephosphorylation of PPDK lead to its inactivation and activation, respectively. Light intensity rather than the light/dark transition regulates PPDK activity by modulating the reversible phosphorylation at Thr527 of PPDK in Zea mays. PDRP catalyzes the reversible phosphorylation of PPDK rapidly and efficiently, but a subtle conformational change around PPDK's active site Thr527 will affect its catalytic efficiency. Analysis by high-resolution mass spectrometry Zea mays
2.7.9.1 phosphoprotein in C4 plants, pyruvate orthophosphate dikinase (PPDK) activity is tightly dark/light regulated by reversible phosphorylation of an active-site Thr residue, catalyzed by PPDK regulatory protein (PDRP). Phosphorylation and dephosphorylation of PPDK lead to its inactivation and activation, respectively. Light intensity rather than the light/dark transition regulates PPDK activity by modulating the reversible phosphorylation at Thr527 of PPDK in Zea mays. PDRP catalyzes the reversible phosphorylation of PPDK rapidly and efficiently, but a subtle conformational change around PPDK's active site Thr527 will affect its catalytic efficiency. Phosphorylation at Thr527 of PPDK is independent of the light/dark transition. The plastidic isozyme shows phosphorylation at four serine (Ser)/Thr residues, Thr527, Ser528, Thr309, and Ser506 are targets of PDRP. The two hydrogen bonds between the highly conserved residues Ser528 and Gly525 are required for PDRP-mediated phosphorylation of the active-site Thr527 of the isozyme. Analysis by high resolution mass spectrometry, locations of the four phosphorylation residues in the primary sequence and the three-dimensional structure of C4PPDK, modelling, overview Zea mays

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.9.1 native isozymes from leaves, subcellular fractionation Zea mays
2.7.9.1 native isozymes from leaves, subcellular fractionation, recombinant tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (RIL) by immobilized metal affinity chromatography Zea mays
2.7.11.32 recombinant His-tagged enzyme from Escherichia coli Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.4.27 leaf isozyme C4ppdk is specifically expressed in maize leaves Zea mays
-
2.7.9.1 leaf
-
 Zea mays
-
2.7.9.1 leaf isozyme C4PPDK is especially expressed in leaves Zea mays
-
2.7.9.1 seedling
-
 Zea mays
-
2.7.11.32 leaf
-
 Zea mays
-
2.7.11.32 mesophyll
-
 Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.27 [pyruvate, phosphate dikinase] phosphate + phosphate
-
 Zea mays [pyruvate, phosphate dikinase] + diphosphate reversible phosphorylation at Thr527 by maize pyruvate orthophosphate dikinase regulatory protein. The level of C4PPDK phosphorylated at Ser528 is much lower than that at Thr527 in maize leaves, meaning that phosphorylation at Ser528 is not as important as at Thr527 for the regulation of PPDK activity. The bifunctional enzyme exhibits kinase activity, EC 2.7.11.32, and dephosphorylation activity, EC 2.7.4.27 ?
2.7.4.27 [pyruvate, phosphate dikinase] phosphate + phosphate
-
 Zea mays [pyruvate, phosphate dikinase] + diphosphate reversible phosphorylation by maize pyruvate orthophosphate dikinase regulatory protein. Residues Thr527 and Ser528, but not Thr309 and Ser506, are targets of PDRP. The bifunctional enzyme exhibits kinase activity, EC 2.7.11.32, and dephosphorylation activity, EC 2.7.4.27 ?
2.7.9.1 ATP + pyruvate + phosphate
-
 Zea mays AMP + phosphoenolpyruvate + diphosphate
-
 r
2.7.11.32 ADP + [pyruvate, phosphate dikinase] reversible phosphorylation at Thr527 and Ser528, but not Thr309 and Ser506, of PPDK Zea mays AMP + [pyruvate, phosphate dikinase] phosphate
-
 r
2.7.11.32 ADP + [pyruvate, phosphate dikinase] i.e. recombinant His-tagged wild-type and mutant maize PPDKs as substrates, reversible phosphorylation at Thr527 and Ser528, but not Thr309 and Ser506, of PPDK. Phosphorylation is detected on wild-type PPDK, PPDK-T309A, and PPDK-S506A, but not on PPDK-T527A, PPDK-S528A, or PPDK-H529A Zea mays AMP + [pyruvate, phosphate dikinase] phosphate
-
 r
2.7.11.32 additional information PPDK regulatory protein (PDRP) is a unique bifunctional enzyme, catalyzes this light-dependent regulation by reversible phosphorylation of an active-site Thr527 in PPDK Zea mays ?
-
 ?
2.7.11.32 additional information modeling suggests that the two hydrogen bonds between the highly conserved residues Ser528 and Gly525 are required for PDRP-mediated phosphorylation of the active-site Thr527 of PPDK, substrate PPDK three-dimensional structure analysis, overview Zea mays ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.27 C4 chloroplast PPDK
-
 Zea mays
2.7.4.27 C4ppdk
-
 Zea mays
2.7.4.27 PDRP
-
 Zea mays
2.7.4.27 PDRP1
-
 Zea mays
2.7.4.27 PPDK regulatory protein
-
 Zea mays
2.7.9.1 C4ppdk
-
 Zea mays
2.7.9.1 C4ppdkZm1
-
 Zea mays
2.7.9.1 Cyppdk
-
 Zea mays
2.7.9.1 CyppdkZm2
-
 Zea mays
2.7.9.1 PPDK
-
 Zea mays
2.7.9.1 PPDK1
-
 Zea mays
2.7.9.1 PPDK2
-
 Zea mays
2.7.9.1 pyruvate orthophosphate dikinase
-
 Zea mays
2.7.11.32 PDRP
-
 Zea mays
2.7.11.32 PPDK regulatory protein
-
 Zea mays

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.9.1 30
-
 assay at Zea mays

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.9.1 8
-
 assay at Zea mays

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.9.1 AMP
-
 Zea mays
2.7.9.1 ATP
-
 Zea mays
2.7.11.32 ADP
-
 Zea mays
2.7.11.32 AMP
-
 Zea mays

General Information

EC Number General Information Comment Organism
2.7.4.27 evolution two loci for PPDK genes in maize chromosomes: one locus can transcribe two overlapping genes (C4 chloroplast PPDK [C4ppdk] and cytosolic PPDK [CyppdkZm1]) that are divergent at their 5' ends owing to different transcription initiation sites, isozyme sequences comparisons, the two peptides differ by 42 D, overview Zea mays
2.7.4.27 additional information the two hydrogen bonds between the highly conserved residues Ser528 and Gly525 are required for enzyme PDRP-mediated phosphorylation of the active site residue Thr527 of PPDK Zea mays
2.7.4.27 physiological function in C4 plants, pyruvate orthophosphate dikinase (PPDK) activity is tightly dark/light regulated by reversible phosphorylation of an active-site threonine residue catalyzed by PPDK regulatory protein (PDRP). Phosphorylation and dephosphorylation of PPDK lead to its inactivation and activation of PPDK, respectively. Light intensity rather than the light/dark transition regulates PPDK activity by modulating the reversible phosphorylation at Thr527 of PPDK in Zea mays. The amount of unphosphorylated PPDK involved in C4 photosynthesis is strictly controlled by light intensity, despite the high levels of PPDK protein that accumulate in mesophyll chloroplasts. The regulation of maize plastid PPDK isoform (C4PPDK) activity is complex, overview Zea mays
2.7.9.1 physiological function PPDK is the key enzyme of the C4 pathway, and its activity may limit the photosynthesis rate in maize leaves. The amount of PPDK (unphosphorylated) involved in C4 photosynthesis is strictly controlled by light intensity Zea mays
2.7.9.1 physiological function PPDK is the key enzyme of the C4 pathway, and its activity may limit the photosynthesis rate in maize leaves. The amount of PPDK (unphosphorylated) involved in C4 photosynthesis is strictly controlled by light intensity. Diverse regulatory pathways may work alone or in combination to fine-tune C4PPDK activity in response to changes in light Zea mays
2.7.11.32 additional information catalytic mechanism of enzyme PDRP, overview Zea mays
2.7.11.32 physiological function in C4 plants, pyruvate orthophosphate dikinase (PPDK) activity is tightly dark/light regulated by reversible phosphorylation of an active-site threonine residue. The process is catalyzed by PPDK regulatory protein (PDRP). Phosphorylation and dephosphorylation of PPDK lead to its inactivation and activation, respectively. The amount of PPDK (unphosphorylated) involved in C4 photosynthesis is indeed strictly controlled by light intensity, despite the high levels of PPDK protein that accumulate in mesophyll chloroplasts, regulation by light intensity rather than the light/dark transition. Diverse regulatory pathways may work alone or in combination to fine-tune C4PPDK activity in response to changes in lighting. Residue Ser528 plays an essential role in PDRP regulation of PPDK phosphorylation at Thr527 Zea mays