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Literature summary for 4.2.1.3 extracted from

  • De Bellis, L.; Tsugeki, R.; Alpi, A.; Nishimura, M.
    Purification and characterization of aconitase isoforms from etiolated pumpkin cotyledons (1993), Physiol. Plant., 99, 485-492.
No PubMed abstract available
Search for more literature for 4.2.1.3

General Stability

General Stability Organism
freezing and thawing inactivates aconitase in absence of glycerol or sucrose Cucurbita sp.

Inhibitors

Inhibitors Comment Organism Structure
Fluorocitrate competitive Cucurbita sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
glyoxysome very low activity Cucurbita sp. 9514
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
89000
-
 1 * 89000, isoenzyme Aco I and Aco II, SDS-PAGE Cucurbita sp.
100000
-
 isoenzyme Aco I and Aco II, gel filtration Cucurbita sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Cucurbita sp. enzyme is involved in the glyoxylate cycle ?
-
 ?

Organism

Organism UniProt Comment Textmining
Cucurbita sp.
-
 3 isoforms: Aco I, Aco II and Aco III
-

Purification (Commentary)

Purification (Comment) Organism
isoenzymes Aco I and Aco II Cucurbita sp.

Source Tissue

Source Tissue Comment Organism Textmining
cotyledon etiolated Cucurbita sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.126
-
 isoenzyme Aco II Cucurbita sp.
2.214
-
 isoenzyme Aco I Cucurbita sp.

Storage Stability

Storage Stability Organism
-20°C, 25% w/v glycerol, stable for several weeks Cucurbita sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme is involved in the glyoxylate cycle Cucurbita sp. ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 89000, isoenzyme Aco I and Aco II, SDS-PAGE Cucurbita sp.