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Literature summary for 4.1.1.48 extracted from

  • Schlee, S.; Klein, T.; Schumacher, M.; Nazet, J.; Merkl, R.; Steinhoff, H.J.; Sterner, R.
    Relationship of Catalysis and Active Site Loop Dynamics in the (betaalpha)8 barrel enzyme indole-3-glycerol phosphate synthase (2018), Biochemistry, 57, 3265-3277 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular dynamics simulations of wild-type at 25°C in the apo form and in the presence of the substrate Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
F246S mutation at C-terminus, increases flexibility Saccharolobus solfataricus
G212E mutation interferes with phosphate binding Saccharolobus solfataricus
L236Q mutation destabilizes helix alpha8' Saccharolobus solfataricus
M237T mutation destabilizes helix alpha8' Saccharolobus solfataricus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000085
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate wild-type, pH 7.5, 25°C Saccharolobus solfataricus
0.000105
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate wild-type, pH 7.5, 60°C Saccharolobus solfataricus
0.0013
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant F246S, pH 7.5, 25°C Saccharolobus solfataricus
0.0029
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant M237T, pH 7.5, 25°C Saccharolobus solfataricus
0.0034
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant L236Q, pH 7.5, 25°C Saccharolobus solfataricus
0.0217
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant G212E, pH 7.5, 25°C Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q06121
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Saccharolobus solfataricus 1-(3-indolyl)glycerol-3-phosphate + CO2 + H2O
-
?
additional information a different degree of loop mobility correlates with different rate-limiting steps in the catalytic mechanism. Both the application of activating mutations and temperature increase lead to a net increase in the catalytic turnover number due to acceleration of the product release rate relative to the chemical transformation steps Saccharolobus solfataricus ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.11
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate wild-type, pH 7.5, 25°C Saccharolobus solfataricus
0.16
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant G212E, pH 7.5, 25°C Saccharolobus solfataricus
0.2
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant L236Q, pH 7.5, 25°C Saccharolobus solfataricus
0.23
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant M237T, pH 7.5, 25°C Saccharolobus solfataricus
0.32
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant F246S, pH 7.5, 25°C Saccharolobus solfataricus
2.1
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate wild-type, pH 7.5, 60°C Saccharolobus solfataricus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
10
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant G212E, pH 7.5, 25°C Saccharolobus solfataricus
60
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant L236Q, pH 7.5, 25°C Saccharolobus solfataricus
80
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant M237T, pH 7.5, 25°C Saccharolobus solfataricus
240
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate mutant F246S, pH 7.5, 25°C Saccharolobus solfataricus
1180
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate wild-type, pH 7.5, 25°C Saccharolobus solfataricus
20000
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate wild-type, pH 7.5, 60°C Saccharolobus solfataricus