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Literature summary for 2.7.1.71 extracted from

  • Krell, T.; Maclean, J.; Boam, D.J.; Cooper, A.; Resmini, M.; Brocklehurst, K.; Kelly, S.M.; Price, N.C.; Lapthorn, A.J.; Coggins, J.R.
    Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine (2001), Protein Sci., 10, 1137-1149.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant enzyme expressed in Escherichia coli Dickeya chrysanthemi

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzyme K15M, sitting-drop vapor diffusion Dickeya chrysanthemi

Protein Variants

Protein Variants Comment Organism
C13S enzymatically active mutant, turnover-number is 65% of that of the wild-type enzyme Dickeya chrysanthemi
C162S turnover-number is 1.14fold higher than that of the wild-type enzyme Dickeya chrysanthemi
D34N inactive mutant enzyme Dickeya chrysanthemi
K15M inactive mutant enzyme, increased thermostability and affinity for ATP when compared to the wild-type enzyme, the organization of the P-loop and flanking regions is heavily disturbed Dickeya chrysanthemi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.075
-
 shikimate pH 7.0, 25°C, mutant enzyme C13S Dickeya chrysanthemi
0.28
-
 shikimate pH 7.0, 25°C, mutant enzyme C162S Dickeya chrysanthemi
0.67
-
 ATP pH 7.0, 25°C, mutant enzyme C162S Dickeya chrysanthemi

Organism

Organism UniProt Comment Textmining
Dickeya chrysanthemi
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + shikimate = ADP + 3-phosphoshikimate the enzyme binds substrates randomly and in a synergistic fashion Dickeya chrysanthemi
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + shikimate
-
 Dickeya chrysanthemi ADP + shikimate 3-phosphate
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 midpoint of protein unfolding transition is 39.7°C for the wild-type enzyme, 39°C for the mutant enzyme C13S and 43.0°C for the wild-type enzyme K15M in absence of ligands Dickeya chrysanthemi

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
23
-
 ATP pH 7.0, 25°C, mutant enzyme C13S Dickeya chrysanthemi
23
-
 shikimate pH 7.0, 25°C, mutant enzyme C13S Dickeya chrysanthemi
35
-
 ATP pH 7.0, 25°C, wild-type enzyme Dickeya chrysanthemi
35
-
 shikimate pH 7.0, 25°C, wild-type enzyme Dickeya chrysanthemi
40
-
 ATP pH 7.0, 25°C, mutant enzyme C162S Dickeya chrysanthemi
40
-
 shikimate pH 7.0, 25°C, mutant enzyme C162S Dickeya chrysanthemi