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Literature summary for 1.4.1.14 extracted from

  • Cordovilla, M.P.; Perez, J.; Ligero, F.; Lluch, C.; Valpuesta, V.
    Partial purification and characterization of NADH-glutamate synthase from faba bean (Vicia faba) root nodules (2000), Plant Sci., 150, 121-128.
No PubMed abstract available

General Stability

General Stability Organism
instability of enzyme during purification process Vicia faba

Metals/Ions

Metals/Ions Comment Organism Structure
3Fe-4S-center enzyme contains non-heme iron and acid-labile sulfur Vicia faba

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
195000
-
1 * 195000, SDS-PAGE Vicia faba
222000
-
gel filtration Vicia faba
236000
-
native PAGE Vicia faba

Organism

Organism UniProt Comment Textmining
Vicia faba
-
-
-

Purification (Commentary)

Purification (Comment) Organism
74fold partial purification Vicia faba

Source Tissue

Source Tissue Comment Organism Textmining
additional information not found in crude soluble protein fractions from leaves or bacteroids Vicia faba
-
root nodule
-
Vicia faba
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.66
-
-
Vicia faba

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 2-oxoglutarate + NADH
-
Vicia faba L-glutamate + NAD+
-
?

Subunits

Subunits Comment Organism
monomer 1 * 195000, SDS-PAGE Vicia faba

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Vicia faba

Cofactor

Cofactor Comment Organism Structure
flavin flavoprotein Vicia faba
NADH
-
Vicia faba