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Literature summary for 5.2.1.8 extracted from

  • Kaur, G.; Singh, S.; Singh, H.; Chawla, M.; Dutta, T.; Kaur, H.; Bender, K.; Snedden, W.A.; Kapoor, S.; Pareek, A.; Singh, P.
    Characterization of peptidyl-prolyl cis-trans isomerase- and calmodulin-binding activity of a cytosolic Arabidopsis thaliana cyclophilin AtCyp19-3 (2015), PLoS ONE, 10, e0136692 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.2.1.8

Cloned(Commentary)

Cloned (Comment) Organism
-
 Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular modeling of structure Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
 Arabidopsis thaliana
cyclosporin A
-
 Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ in vitro interaction with calmodulin is Ca2+-dependent Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q38867
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
 Arabidopsis thaliana N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
 ?

Subunits

Subunits Comment Organism
? x * 23000, SDS-PAGE, 18920, calculated from sequence, His-tagged recombinant protein Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
At3g56070
-
 Arabidopsis thaliana
Cyp19-3
-
 Arabidopsis thaliana

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.036
-
 N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide pH 8.0, 15°C Arabidopsis thaliana

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0000188
-
 cyclosporin A pH 8.0, 15°C Arabidopsis thaliana

General Information

General Information Comment Organism
physiological function enzyme interacts with calmodulin in vivo and in vitro. In vitro interaction is Ca2+-dependent, and the calmodulin-binding domain is localized to 35-70 amino acid residues in the N-terminus Arabidopsis thaliana