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Literature summary for 2.3.3.16 extracted from

  • Takeda, T.; Kurasawa, Y.; Watanabe, Y.; Numata, O.
    Polymerization of highly purified Tetrahymena 14-nm filament protein/citrate synthase into filaments and its possible roles in regulation of enzymatic activity (1995), J. Biochem., 117, 869-874.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
elongation factor 1alpha causes polymerization of 49K protein, reduced activity Tetrahymena pyriformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + oxaloacetate + H2O Tetrahymena pyriformis also acting as structural protein in oral morphogenesis and conjugation citrate + CoA
-
?

Organism

Organism UniProt Comment Textmining
Tetrahymena pyriformis
-
identical with 14-nm filament protein, i.e. 49K protein
-

Purification (Commentary)

Purification (Comment) Organism
-
Tetrahymena pyriformis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
activity increased by depolymerization, decreased by polymerization, possible mode of regulation Tetrahymena pyriformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + oxaloacetate + H2O
-
Tetrahymena pyriformis citrate + CoA
-
?
acetyl-CoA + oxaloacetate + H2O also acting as structural protein in oral morphogenesis and conjugation Tetrahymena pyriformis citrate + CoA
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Tetrahymena pyriformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Tetrahymena pyriformis