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Literature summary extracted from

  • Sagami, H.; Ogura, K.
    Multiple forms of isopentenyl pyrophosphate isomerase of avian liver (1983), J. Biochem., 94, 975-979.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.3.3.2 2-mercaptoethanol activates isomerase III and IV Gallus gallus

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.3.2 diphosphate inhibitory effect decreases in the order of isomerases I, II, III, and IV Gallus gallus
5.3.3.2 iodoacetamide inhibitory effect decreases in the order of isomerases I, II, III, no inhibition of isomerase IV Gallus gallus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.3.2 0.0013
-
 isopentenyl diphosphate isomerase II and III Gallus gallus
5.3.3.2 0.0017
-
 isopentenyl diphosphate isomerase I Gallus gallus
5.3.3.2 0.0025
-
 isopentenyl diphosphate isomerase IV Gallus gallus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.3.2 Co2+ slight activation Gallus gallus
5.3.3.2 Mg2+ slight activation Gallus gallus
5.3.3.2 Mn2+ isomerase I: maximal activation at 0.5 mM, isomerase II, III or IV: maximal activation at 0.25 mM Gallus gallus
5.3.3.2 Ni2+ slight activation Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
5.3.3.2 Gallus gallus
-
 4 enzyme forms: I, II, III, and IV
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.3.3.2 liver
-
 Gallus gallus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.3.2 isopentenyl diphosphate
-
 Gallus gallus dimethylallyl diphosphate
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.3.2 6.6
-
-
 Gallus gallus