Literature summary for 2.7.9.1 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.

Search for more literature for 2.7.9.1

Cloned(Commentary)

Cloned (Comment)	Organism
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
gene CyppdkZm2, quantitative real-time PCR enzyme expression analysis	Zea mays

Protein Variants

Protein Variants	Comment	Organism
G525A	site-directed mutagenesis, the mutant shows no phosphorylation signal	Zea mays
G525P	site-directed mutagenesis, the mutant shows no phosphorylation signal	Zea mays
H529A	site-directed mutagenesis	Zea mays
S506A	site-directed mutagenesis	Zea mays
S528A	site-directed mutagenesis	Zea mays
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
S528D	site-directed mutagenesis	Zea mays
S528T	site-directed mutagenesis, the mutant shows no phosphorylation signal	Zea mays
S528Y	site-directed mutagenesis, the mutant shows no phosphorylation signal	Zea mays
T309A	site-directed mutagenesis	Zea mays
T527A	site-directed mutagenesis	Zea mays
T527D	site-directed mutagenesis	Zea mays

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
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	-
cytosol	the mature isozyme CyPPDKZm1 contains the 11-residue sequence MAPAPCGRSSQ	Zea mays	5829	-
soluble	-	Zea mays	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + pyruvate + phosphate	Zea mays	-	AMP + phosphoenolpyruvate + diphosphate	-	r

Organism

Organism	UniProt	Comment	Textmining
Zea mays	P11155	ecotype B73	-
Zea mays	Q42368	ecotype B73	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	partial amino-terminal acetylation of the plastidic isozyme	Zea mays
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
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)

Purification (Comment)	Organism
native isozymes from leaves, subcellular fractionation	Zea mays
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

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Zea mays	-
leaf	isozyme C4PPDK is especially expressed in leaves	Zea mays	-
seedling	-	Zea mays	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + pyruvate + phosphate	-	Zea mays	AMP + phosphoenolpyruvate + diphosphate	-	r

Synonyms

Synonyms	Comment	Organism
C4ppdk	-	Zea mays
C4ppdkZm1	-	Zea mays
Cyppdk	-	Zea mays
CyppdkZm2	-	Zea mays
PPDK	-	Zea mays
PPDK1	-	Zea mays
PPDK2	-	Zea mays
pyruvate orthophosphate dikinase	-	Zea mays

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor	Comment	Organism	Structure
AMP	-	Zea mays
ATP	-	Zea mays

General Information

General Information	Comment	Organism
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
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

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Release 2023.1 (January 2023)