Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kim, J.Y.; Kinoshita, M.; Kume, S.; Gt, H.; Sugiki, T.; Ladbury, J.E.; Kojima, C.; Ikegami, T.; Kurisu, G.; Goto, Y.; Hase, T.; Lee, Y.H.
    Non-covalent forces tune the electron transfer complex between ferredoxin and sulfite reductase to optimize enzymatic activity (2016), Biochem. J., 473, 3837-3854 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.7.1 expression in Escherichia coli Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.7.1 chloroplast
-
Zea mays 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.7.1 NaCl at 40-70 mM NaCl in 50 mM Tris/HCl buffer, close to the physiological conditions in plant chloroplasts, delicate interprotein regulation optimizes SiR activity. At NaCl concentrations above several hundred millimolar, collision and diffusion may limit the formation of the stable electron-transfer competent complex Zea mays

Organism

EC Number Organism UniProt Comment Textmining
1.8.7.1 Zea mays O23813
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.7.1 leaf
-
Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.7.1 additional information ferredoxin:SiR complex formation and interprotein affinity are thermodynamically adjusted by both enthalpy and entropy through electrostatic and non-electrostatic interactions. A combination of electrostatic and non-electrostatic forces stabilizes the complex with similar interfaces and modulates the binding affinity and mode Zea mays ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.8.7.1 SIR
-
Zea mays