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Literature summary for 2.5.1.19 extracted from

  • Zhang, Y.; Yi, L.; Lin, Y.; Zhang, L.; Shao, Z.; Liu, Z.
    Characterization and site-directed mutagenesis of a novel class II 5-enopyruvylshikimate-3-phosphate (EPSP) synthase from the deep-sea bacterium Alcanivorax sp. L27 (2014), Enzyme Microb. Technol., 63, 64-70.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells Alcanivorax sp.

Protein Variants

Protein Variants Comment Organism
G100A the mutant has a 30fold increase in the IC50 value for glyphosate and slightly reduced specific activity compared to the wild type enzyme Alcanivorax sp.
L105P the mutant shows 20% catalytic activity compared to wild type enzyme Alcanivorax sp.

Inhibitors

Inhibitors Comment Organism Structure
glyphosate
-
Alcanivorax sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.078
-
phosphoenolpyruvate wild type enzyme, at pH 7.0 and 28°C Alcanivorax sp.
0.169
-
3-phosphoshikimate wild type enzyme, at pH 7.0 and 28°C Alcanivorax sp.
0.227
-
phosphoenolpyruvate mutant enzyme G100A, at pH 7.0 and 28°C Alcanivorax sp.
0.706
-
3-phosphoshikimate mutant enzyme G100A, at pH 7.0 and 28°C Alcanivorax sp.
4.762
-
phosphoenolpyruvate mutant enzyme L105P, at pH 7.0 and 28°C Alcanivorax sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
x * 45000, SDS-PAGE Alcanivorax sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphoenolpyruvate + 3-phosphoshikimate Alcanivorax sp.
-
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
r
phosphoenolpyruvate + 3-phosphoshikimate Alcanivorax sp. L27
-
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
r

Organism

Organism UniProt Comment Textmining
Alcanivorax sp.
-
-
-
Alcanivorax sp. L27
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Alcanivorax sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.76
-
mutant enzyme L105P, at pH 7.0 and 28°C Alcanivorax sp.
7.26
-
mutant enzyme G100A, at pH 7.0 and 28°C Alcanivorax sp.
7.78
-
wild type enzyme, at pH 7.0 and 28°C Alcanivorax sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + 3-phosphoshikimate
-
Alcanivorax sp. phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
r
phosphoenolpyruvate + 3-phosphoshikimate
-
Alcanivorax sp. L27 phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
r

Subunits

Subunits Comment Organism
? x * 45000, SDS-PAGE Alcanivorax sp.
? x * 45954, calculated from amino acid sequence Alcanivorax sp.

Synonyms

Synonyms Comment Organism
3-phosphoshikimate-1-carboxyvinyl-transferase
-
Alcanivorax sp.
5-enopyruvylshikimate-3-phosphate synthase
-
Alcanivorax sp.
AroA
-
Alcanivorax sp.
EPSP synthase
-
Alcanivorax sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Alcanivorax sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
-
60 the enzyme retains 20% of its activity at 0°C and 60°C, respectively, and shows about 45% activity at 20°C and about 90% at 40°C Alcanivorax sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Alcanivorax sp.

pH Range

pH Minimum pH Maximum Comment Organism
5.5 8 more than 80% of the activity is retained between pH 5.5 and pH 8.0 Alcanivorax sp.

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.5
-
wild type enzyme, at pH 7.0 and 28°C Alcanivorax sp. glyphosate
45.2
-
mutant enzyme G100A, at pH 7.0 and 28°C Alcanivorax sp. glyphosate