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Literature summary for 2.7.1.19 extracted from

  • Runquist, J.A.; Harrison, D.H.; Miziorko, H.M.
    Functional evaluation of invariant arginines situated in the mobile lid domain of phosphoribulokinase (1998), Biochemistry, 37, 1221-1226.
    View publication on PubMed
Search for more literature for 2.7.1.19

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutants Cereibacter sphaeroides

Protein Variants

Protein Variants Comment Organism
R168Q 300fold decrease in catalytic efficiency, 50fold increased Km for D-ribulose 5-phosphate Cereibacter sphaeroides
R173Q 100fold increased Km for D-ribulose 5-phosphate Cereibacter sphaeroides
R186Q decreased Km for D-ribulose 5-phosphate Cereibacter sphaeroides
R187Q increased Km for D-ribulose 5-phosphate Cereibacter sphaeroides

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.048
-
 D-ribulose 5-phosphate R186Q mutant, pH 8, 30°C Cereibacter sphaeroides
0.096
-
 D-ribulose 5-phosphate wild-type enzyme, pH 8, 30°C Cereibacter sphaeroides
0.55
-
 D-ribulose 5-phosphate R187Q mutant, pH 8, 30°C Cereibacter sphaeroides
4.6
-
 D-ribulose 5-phosphate R168Q mutant, pH 8, 30°C Cereibacter sphaeroides
10.5
-
 D-ribulose 5-phosphate R173Q mutant, pH 8, 30°C Cereibacter sphaeroides

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Cereibacter sphaeroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-ribulose 5-phosphate + ATP
-
 Cereibacter sphaeroides D-ribulose 1,5-diphosphate + ADP
-
 ?
D-ribulose 5-phosphate + trinitrophenyl-ATP
-
 Cereibacter sphaeroides D-ribulose 1,5-diphosphate + trinitrophenyl-ADP
-
 ?