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Literature summary for 5.4.99.5 extracted from

  • Singh, B.K.; Connelly, J.A.; Conn, E.E.
    Chorismate mutase isoenzymes from Sorghum bicolor: purification and properties (1985), Arch. Biochem. Biophys., 243, 374-384.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
L-Trp activates Sorghum bicolor
L-Trp enzyme form CM2 is unaffected Sorghum bicolor

Inhibitors

Inhibitors Comment Organism Structure
L-Phe enzyme form CM1 is inhibited; enzyme form CM2 is not inhibited Sorghum bicolor
L-Tyr enzyme form CM2 is not inhibited Sorghum bicolor

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
enzyme form CM2, gel filtration Sorghum bicolor
56000
-
enzyme form CM1, gel filtration Sorghum bicolor

Organism

Organism UniProt Comment Textmining
Sorghum bicolor
-
2 enzyme forms: CM1 and CM2
-

Purification (Commentary)

Purification (Comment) Organism
enzyme form CM1 and CM2 Sorghum bicolor

Source Tissue

Source Tissue Comment Organism Textmining
culm
-
Sorghum bicolor
-
kernel
-
Sorghum bicolor
-
leaf
-
Sorghum bicolor
-
seedling green or etiolated Sorghum bicolor
-

Storage Stability

Storage Stability Organism
0°C or -20°C, enzyme forms CM1 and CM2, stable for at least 6 weeks Sorghum bicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Chorismate
-
Sorghum bicolor Prephenate
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
pH 9.0, 5 min, enzyme form CM2, 15% loss of activity Sorghum bicolor
60
-
pH 9.0, 5 min, stable up to Sorghum bicolor

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 10 enzyme form CM1 Sorghum bicolor
7.5 9.5 enzyme form CM2 Sorghum bicolor