Literature summary for 2.7.9.1 extracted from

Lim, K.; Read, R.J.; Chen, C.C.; Tempczyk, A.; Wei, M.; Ye, D.; Wu, C.; Dunaway-Mariano, D.; Herzberg, O.
Swiveling domain mechanism in pyruvate phosphate dikinase (2007), Biochemistry, 46, 14845-14853.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of mutant enzyme R219E/E271R/S262D in Escherichia coli strain JM101	[Clostridium] symbiosum

Crystallization (Commentary)

Crystallization (Comment)	Organism
PPDK, mutant R219E/E271R/S262D, hanging drop vapour diffusion method at 30°C, using a protein solution containing 28 mg/ml protein in 20 mM imidazole, pH 6.5, 0.1 mM EDTA, 100 mM KCl, and 1 mM DTT. The reservoir solution contains 50% saturated ammonium sulfate and 0.1 M Na-HEPES, pH 7.0, mixing of equal volumes of protein solution and reservoir solution, structure determination and analysis of two different enzyme conformations at 1.94 A resolution, modeling	[Clostridium] symbiosum

Crystallization (Comment)

Organism

PPDK, mutant R219E/E271R/S262D, hanging drop vapour diffusion method at 30°C, using a protein solution containing 28 mg/ml protein in 20 mM imidazole, pH 6.5, 0.1 mM EDTA, 100 mM KCl, and 1 mM DTT. The reservoir solution contains 50% saturated ammonium sulfate and 0.1 M Na-HEPES, pH 7.0, mixing of equal volumes of protein solution and reservoir solution, structure determination and analysis of two different enzyme conformations at 1.94 A resolution, modeling

[Clostridium] symbiosum

Protein Variants

Protein Variants	Comment	Organism
R219E/E271R/S262D	site-directed mutagensis, comparison of mutant to wild-type enzyme structure	[Clostridium] symbiosum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	single-turnover reaction kinetics, mutant R219E/E271R/S261D	[Clostridium] symbiosum

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	[Clostridium] symbiosum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
AMP + phosphoenolpyruvate + diphosphate	[Clostridium] symbiosum	-	ATP + pyruvate + phosphate	-	r

Organism

Organism	UniProt	Comment	Textmining
[Clostridium] symbiosum	P22983	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
AMP + phosphoenolpyruvate + diphosphate	-	[Clostridium] symbiosum	ATP + pyruvate + phosphate	-	r
AMP + phosphoenolpyruvate + diphosphate	PPDK catalyzes the reversible conversion of phosphoenolpyruvate, AMP, and phosphate to pyruvate and ATP, phosphoryl group transfer between PEP and His455, structure and mechanism, overview	[Clostridium] symbiosum	ATP + pyruvate + phosphate	-	r
additional information	swiveling domain mechanism in pyruvate phosphate dikinase, upon detachment from the His domain, the two nucleotide-binding subdomains undergo a hinge motion that opens the active-site cleft, the nucleotide-binding domain undergoes a conformational transition upon binding of Mg2+, ATP, and phosphate, overview	[Clostridium] symbiosum	?	-	?

Subunits

Subunits	Comment	Organism
More	PPDK contains a His445-containing domain, which is positioned close to the nucleotide binding domain and does not contact the PEP/pyruvate-binding domain, the enzyme shows two conformations and swivel motion of the His domain, upon detachment from the His domain, the two nucleotide-binding subdomains undergo a hinge motion that opens the active-site cleft, structure analysis, overview	[Clostridium] symbiosum

Synonyms

Synonyms	Comment	Organism
PPDK	-	[Clostridium] symbiosum
pyruvate phosphate dikinase	-	[Clostridium] symbiosum

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	[Clostridium] symbiosum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.8	7	assay at	[Clostridium] symbiosum

Cofactor

Cofactor	Comment	Organism	Structure
AMP	forward reaction	[Clostridium] symbiosum
ATP	reverse reaction	[Clostridium] symbiosum