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Literature summary for 2.7.4.27 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
Search for more literature for 2.7.4.27

Cloned(Commentary)

Cloned (Comment) Organism
recombinant overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) RIL Zea mays

Protein Variants

Protein Variants Comment Organism
G525A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
G525P site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
H529A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
S506A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
S528A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
S528C site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
S528D site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
S528T site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
S528Y site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
T309A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
T527A site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays
T527D site-directed mutagenesis of a C4PPDK phosphorylation site Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast the enzyme contains a transit peptide cleavage site Zea mays 9507
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[pyruvate, phosphate dikinase] phosphate + phosphate Zea mays
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 [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 ?

Organism

Organism UniProt Comment Textmining
Zea mays Q195N6 isozyme C4 chloroplast PPDK, i.e. C4ppdk, gene PDRP1
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme contains a transit peptide cleavage site Zea mays
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

Source Tissue

Source Tissue Comment Organism Textmining
leaf isozyme C4ppdk is specifically expressed in maize leaves Zea mays
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[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 ?
[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 ?

Synonyms

Synonyms Comment Organism
C4 chloroplast PPDK
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 Zea mays
C4ppdk
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 Zea mays
PDRP
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 Zea mays
PDRP1
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 Zea mays
PPDK regulatory protein
-
 Zea mays

General Information

General Information Comment Organism
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
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
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