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

BRENDA support

Literature summary extracted from

  • Sakakibara, Y.; Kimura, H.; Iwamura, A.; Saitoh, T.; Ikegami, T.; Kurisu, G.; Hase, T.
    A new structural insight into differential interaction of cyanobacterial and plant ferredoxins with nitrite reductase as revealed by NMR and X-ray crystallographic studies (2012), J. Biochem., 151, 483-492.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.7.1 expression in Escherichia coli Synechocystis sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.7.1 NMR-study of protein-protein interaction of ferredoxin and nitrite reductase shows three acidic regions of ferredoxin to be major sites for the interaction with the enzyme, indicating that the complex is stabilized through electrostatic interaction Synechocystis sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.7.1 0.0077
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin mutant E94Q/E95Q, pH 7.5, 25°C Synechocystis sp.
1.7.7.1 0.0097
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin, pH 7.5, 25°C Synechocystis sp.
1.7.7.1 0.0213
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin mutant D67N/D68N/D69N, pH 7.5, 25°C Synechocystis sp.
1.7.7.1 0.0478
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin mutant E31Q/E32Q/D36N, pH 7.5, 25°C Synechocystis sp.
1.7.7.1 0.0746
-
 reduced ferredoxin substrate maize ferredoxin, pH 7.5, 25°C Synechocystis sp.

Organism

EC Number Organism UniProt Comment Textmining
1.7.7.1 Synechocystis sp.
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.7.1 nitrite + 6 reduced ferredoxin
-
 Synechocystis sp. ammonia + 2 H2O + 6 oxidized ferredoxin
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7.7.1 101.4
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin mutant E94Q/E95Q, pH 7.5, 25°C Synechocystis sp.
1.7.7.1 138.2
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin, pH 7.5, 25°C Synechocystis sp.
1.7.7.1 178.3
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin mutant D67N/D68N/D69N, pH 7.5, 25°C Synechocystis sp.
1.7.7.1 203.2
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin mutant E31Q/E32Q/D36N, pH 7.5, 25°C Synechocystis sp.

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.7.7.1 4300
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin mutant E31Q/E32Q/D36N, pH 7.5, 25°C Synechocystis sp.
1.7.7.1 8400
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin mutant D67N/D68N/D69N, pH 7.5, 25°C Synechocystis sp.
1.7.7.1 13200
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin mutant E94Q/E95Q, pH 7.5, 25°C Synechocystis sp.
1.7.7.1 14200
-
 reduced ferredoxin substrate Leptolyngbya boryana ferredoxin, pH 7.5, 25°C Synechocystis sp.