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Literature summary for 2.7.1.63 extracted from

  • Kowalczyk, T.H.; Horn, P.J.; Pan, W.H.; Phillips, N.F.
    Initial rate and equilibrium isotope exchange studies on the ATP-dependent activity of polyphosphate Glucokinase from Propionibacterium shermanii (1996), Biochemistry, 35, 6777-6785.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
ADP inhibits reaction with ATP Propionibacterium freudenreichii subsp. shermanii
D-glucose 6-phosphate inhibits reaction with ATP Propionibacterium freudenreichii subsp. shermanii
D-xylose inhibits reaction with ATP Propionibacterium freudenreichii subsp. shermanii
Tetrapolyphosphate inhibits reaction with ATP Propionibacterium freudenreichii subsp. shermanii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0012
-
(phosphate)31 pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii
0.8
-
GTP pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii
1.2
-
dATP pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii
1.5
-
ATP pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii
2.6
-
UTP pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii
5.9
-
CTP pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii

Organism

Organism UniProt Comment Textmining
Propionibacterium freudenreichii subsp. shermanii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
not separable from ATP-glucokinase Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(phosphate)31 + D-glucose
-
Propionibacterium freudenreichii subsp. shermanii (phosphate)30 + D-glucose 6-phosphate
-
?
(phosphate)n + D-glucose the enzyme utilizes polyphosphate much more efficiently than it does ATP, with a turnover number/Kpolyphosphate to turnover number/KATP ratio of 2800 Propionibacterium freudenreichii subsp. shermanii (phosphate)n-1 + D-glucose 6-phosphate
-
?
ATP + D-glucose the enzyme utilizes polyphosphate much more efficiently than it does ATP, with a turnover number/Kpolyphosphate to turnover number/KATP ratio of 2800 Propionibacterium freudenreichii subsp. shermanii ADP + D-glucose 6-phosphate
-
?
CTP + glucose
-
Propionibacterium freudenreichii subsp. shermanii CDP + D-glucose 6-phosphate
-
?
dATP + glucose
-
Propionibacterium freudenreichii subsp. shermanii dADP + D-glucose 6-phosphate
-
?
GTP + glucose
-
Propionibacterium freudenreichii subsp. shermanii GDP + D-glucose 6-phosphate
-
?
UTP + glucose
-
Propionibacterium freudenreichii subsp. shermanii UDP + D-glucose 6-phosphate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7
-
UTP pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii
7.4
-
CTP pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii
11
-
GTP pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii
14
-
dATP pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii
25
-
ATP pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii
56
-
(phosphate)31 pH 7.5, 30°C Propionibacterium freudenreichii subsp. shermanii