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Literature summary for 1.4.1.14 extracted from

  • Boland, M.J.
    NADH-dependent glutamate synthase from lupin nodules. Reactions with oxidised and reduced 3-acetylpyridine-adenine dinucleotide (1981), Eur. J. Biochem., 115, 485-489.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
3-acetylpyridine adenine dinucleotide competitive inhibitor with respect to NADH Lupinus angustifolius
NADH substrate inhibition at high concentrations Lupinus angustifolius

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0013
-
NADH
-
Lupinus angustifolius
0.0014
-
NADH NADH-dependent reduction of oxidized form of 3-acetylpyridine adenine dinucleotide Lupinus angustifolius
0.003
-
3-acetylpyridine adenine dinucleotide reduced form Lupinus angustifolius
0.006
-
2-oxoglutarate with reduced form of 3-acetylpyridine adenine dinucleotide as reductant Lupinus angustifolius
0.014
-
3-acetylpyridine adenine dinucleotide NADH-dependent reduction of oxidized form of 3-acetylpyridine adenine dinucleotide Lupinus angustifolius
0.024
-
2-oxoglutarate
-
Lupinus angustifolius
0.125
-
L-glutamine with reduced form of 3-acetylpyridine adenine dinucleotide as reductant Lupinus angustifolius
0.5
-
L-glutamine
-
Lupinus angustifolius

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Lupinus angustifolius 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamine + 2-oxoglutarate + NADH Lupinus angustifolius key enzyme in pathway of assimilation of symbiotically fixed N2 into amino acids glutamate + NAD+
-
?

Organism

Organism UniProt Comment Textmining
Lupinus angustifolius
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
root nodule
-
Lupinus angustifolius
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 2-oxoglutarate + NADH NADH binds first before enzyme is capable to bind other substrates Lupinus angustifolius L-glutamate + NAD+
-
?
L-glutamine + 2-oxoglutarate + NADH key enzyme in pathway of assimilation of symbiotically fixed N2 into amino acids Lupinus angustifolius glutamate + NAD+
-
?
L-glutamine + 2-oxoglutarate + reduced form of 3-acetylpyridine adenine dinucleotide reduced form of 3-acetylpyridine adenine dinucleotide is an alternative reductant to NADH, binds as tightly as NADH, enzyme catalyzes NADH-dependent reduction of AcPdAD+ by a substituted-enzyme ping-pong mechanism Lupinus angustifolius L-glutamine + oxidized form of 3-acetylpyridine adenine dinucleotide
-
?
additional information
-
Lupinus angustifolius ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Lupinus angustifolius

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
18
-
3-acetylpyridine adenine dinucleotide reduced form as reductant, glutamate synthase reaction Lupinus angustifolius
51
-
3-acetylpyridine adenine dinucleotide NADH-dependent reduction of oxidized form of 3-acetylpyridine adenine dinucleotide Lupinus angustifolius
70
-
NADH
-
Lupinus angustifolius

Cofactor

Cofactor Comment Organism Structure
3-acetylpyridine adenine dinucleotide reduced form is an alternative reductant, binds as tightly as NADH Lupinus angustifolius
NADH
-
Lupinus angustifolius

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.001
-
3-acetylpyridine adenine dinucleotide
-
Lupinus angustifolius
0.01
-
NADH
-
Lupinus angustifolius