Literature summary for 2.7.4.1 extracted from

Kamatani, S.; Takegawa, K.; Kimura, Y.
Catalytic activity profile of polyphosphate kinase 1 from Myxococcus xanthus (2018), Curr. Microbiol., 75, 379-385 .

Search for more literature for 2.7.4.1

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.32	-	ADP	pH 8.0, 37°C	Myxococcus xanthus
1.23	-	ATP	pH 8.0, 37°C	Myxococcus xanthus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	partially active in the presence of 5 mM Ca2+, 25% compared to activity with 5 mM Mg2+	Myxococcus xanthus
Co2+	partially active in the presence of 5 mM Co2+, 23% compared to activity with 5 mM Mg2+	Myxococcus xanthus
Mg2+	the enzyme requires Mg2+ or Mn2+ for maximum activity. Optimal concentration for polyphosphate synthesis is between 1 and 2.5 mM	Myxococcus xanthus
Mn2+	the enzyme requires Mg2+ or Mn2+ for maximum activity. Optimal concentration for polyphosphate synthesis is 1 mM	Myxococcus xanthus
Zn2+	partially active in the presence of 5 mM Zn2+, 21% compared to activity with 5 mM Mg2+	Myxococcus xanthus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
80400	-	calculated from sequence	Myxococcus xanthus
82000	-	SDS-PAGE	Myxococcus xanthus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ADP + (phosphate)n+1	Myxococcus xanthus	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzed ATP formation	ATP + (phosphate)n	-	r
ADP + (phosphate)n+1	Myxococcus xanthus DK 1622	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzed ATP formation	ATP + (phosphate)n	-	r
ATP + (phosphate)n	Myxococcus xanthus	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzes ATP formation	ADP + (phosphate)n+1	-	r
ATP + (phosphate)n	Myxococcus xanthus DK 1622	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzes ATP formation	ADP + (phosphate)n+1	-	r

Organism

Organism	UniProt	Comment	Textmining
Myxococcus xanthus	Q1DG84	-	-
Myxococcus xanthus DK 1622	Q1DG84	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ADP + (phosphate)n+1	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzed ATP formation	Myxococcus xanthus	ATP + (phosphate)n	-	r
ADP + (phosphate)n+1	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis. GTP and GDP are not recognized as substrates	Myxococcus xanthus	ATP + (phosphate)n	-	r
ADP + (phosphate)n+1	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzed ATP formation	Myxococcus xanthus DK 1622	ATP + (phosphate)n	-	r
ADP + (phosphate)n+1	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis. GTP and GDP are not recognized as substrates	Myxococcus xanthus DK 1622	ATP + (phosphate)n	-	r
ATP + (phosphate)n	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzes ATP formation	Myxococcus xanthus	ADP + (phosphate)n+1	-	r
ATP + (phosphate)n	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis. GTP and GDP are not recognized as substrates	Myxococcus xanthus	ADP + (phosphate)n+1	-	r
ATP + (phosphate)n	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzes ATP formation	Myxococcus xanthus DK 1622	ADP + (phosphate)n+1	-	r
ATP + (phosphate)n	when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis. GTP and GDP are not recognized as substrates	Myxococcus xanthus DK 1622	ADP + (phosphate)n+1	-	r
additional information	in the absence of polyP, the enzyme (Ppk1) generates ATP and AMP from ADP, and ADP from ATP and AMP, suggesting that the enzyme catalyzes the transfer of a phosphate group between ADP molecules yielding ATP and AMP, thus exhibiting adenylate kinase activity	Myxococcus xanthus	?	-	-
additional information	in the absence of polyP, the enzyme (Ppk1) generates ATP and AMP from ADP, and ADP from ATP and AMP, suggesting that the enzyme catalyzes the transfer of a phosphate group between ADP molecules yielding ATP and AMP, thus exhibiting adenylate kinase activity	Myxococcus xanthus DK 1622	?	-	-

Synonyms

Synonyms	Comment	Organism
MXAN_0056	-	Myxococcus xanthus
polyphosphate kinase 1	-	Myxococcus xanthus
PPK1	-	Myxococcus xanthus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	-	Myxococcus xanthus

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
20	50	20°C: about 40% of maximal activity, 50°C: about 65% of maximal activity	Myxococcus xanthus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.56	-	ATP	pH 8.0, 37°C	Myxococcus xanthus
0.58	-	ADP	pH 8.0, 37°C	Myxococcus xanthus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	9	-	Myxococcus xanthus

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.46	-	ATP	pH 8.0, 37°C	Myxococcus xanthus
1.81	-	ADP	pH 8.0, 37°C	Myxococcus xanthus

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Release 2023.1 (January 2023)