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Literature summary for 2.7.1.63 extracted from

  • Hsieh, P.C.; Kowalczyk, T.H.; Phillips, N.F.
    Kinetic mechanisms of polyphosphate glucokinase from Mycobacterium tuberculosis (1996), Biochemistry, 35, 9772-9781.
    View publication on PubMed
Search for more literature for 2.7.1.63

Inhibitors

Inhibitors Comment Organism Structure
ADP inhibits reaction with ATP Mycobacterium tuberculosis
AMP inhibits reaction with polyphosphate and glucose or ATP and glucose Mycobacterium tuberculosis
ATP at high concentrations competitive substrate inhibition with respect to glucose, ATP-dependent reaction Mycobacterium tuberculosis
D-fructose 6-phosphate inhibits reaction with polyphosphate and glucose or ATP and glucose Mycobacterium tuberculosis
D-glucose 6-phosphate inhibits reaction with polyphosphate and glucose Mycobacterium tuberculosis
D-xylose inhibits reaction with ATP; inhibits reaction with polyphosphate and glucose or ATP and glucose Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
 D-glucose pH 7.5, reaction with ATP Mycobacterium tuberculosis
0.22
-
 D-glucose pH 8.6, reaction with ATP Mycobacterium tuberculosis
0.88
-
 ATP pH 7.5 Mycobacterium tuberculosis
1.4
-
 ATP pH 8.6 Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
(phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate in the polyphosphate-dependent reaction the enzyme follows an ordered bi bi sequential mechanism with polyphosphate binding to the enzyme first and glucose 6-phosphate dissociating last. The ATP-dependent glucokinase reaction is consistent with an ordered bi bi sequential mechanism, with ATP binding to the enzyme first and glucose 6-phosphate leaving last Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(phosphate)n + D-glucose polyphosphate is utilized nonprocessively with a preference for longer chains Mycobacterium tuberculosis (phosphate)n-1 + D-glucose 6-phosphate
-
 ?
ATP + D-glucose
-
 Mycobacterium tuberculosis ADP + D-glucose 6-phosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
108
-
 ATP pH 7.5 Mycobacterium tuberculosis
108
-
 glucose pH 7.5 Mycobacterium tuberculosis
116
-
 ATP pH 8.6 Mycobacterium tuberculosis
116
-
 glucose pH 8.6 Mycobacterium tuberculosis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.6
-
 ATP pH 7.5 Mycobacterium tuberculosis
7.4
-
 ATP pH 8.6 Mycobacterium tuberculosis