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

BRENDA support

Literature summary for 1.4.1.14 extracted from

  • Vance, C.P.; Miller, S.S.; Gregerson, D.L.; Samac, D.A.; Robinson, D.L.; Gantt, J.S.
    Alfalfa NADH-dependent glutamate synthase: Structure of the gene and importance in symbiotic N2 fixation (1995), Plant J., 8, 345-358.
    View publication on PubMed
Search for more literature for 1.4.1.14

Cloned(Commentary)

Cloned (Comment) Organism
isolation and characterization of NADH-GOGAT gene with 22 exons and 21 introns, isolation of 7.2 kbp cDNA encoding the complete enzyme Medicago sativa

Localization

Localization Comment Organism GeneOntology No. Textmining
plastid major portion of enzyme activity resides in the plastidial fraction Medicago sativa 9536
-

Metals/Ions

Metals/Ions Comment Organism Structure
3Fe-4S-center flavoprotein containing an iron-sulfur cluster: 3Fe-4S cluster Medicago sativa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
229000
-
 calculated from the cDNA sequence, without N-terminal presequence of 101 amino acids Medicago sativa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamine + 2-oxoglutarate + NADH Medicago sativa root nodule ammonia assimilation, enzyme plays a central role in the functioning of effective root nodules glutamate + NAD+
-
 ?
L-glutamine + 2-oxoglutarate + NADH Medicago sativa predominant enzyme in N2-fixing root nodules and roots, whereas in leaves and cotyledons Fd-GOGAT is the major form of GOGAT involved in nitrogen assimilation, NADH-GOGAT may be a rate-limiting step in NH4+ assimilation in root nodules glutamate + NAD+
-
 ?

Organism

Organism UniProt Comment Textmining
Medicago sativa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification primary translation product is a 240 kDa protein, that contains a N-terminal 101 amino acid presequence resulting in a processed protein of 229 kDa Medicago sativa

Source Tissue

Source Tissue Comment Organism Textmining
additional information little or no enzyme activity and mRNA in leaves, stems, cotyledons and roots Medicago sativa
-
root nodule enzyme activity increases markedly during development of effective root nodules Medicago sativa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 2-oxoglutarate + NADH
-
 Medicago sativa L-glutamate + NAD+
-
 ?
L-glutamine + 2-oxoglutarate + NADH root nodule ammonia assimilation, enzyme plays a central role in the functioning of effective root nodules Medicago sativa glutamate + NAD+
-
 ?
L-glutamine + 2-oxoglutarate + NADH predominant enzyme in N2-fixing root nodules and roots, whereas in leaves and cotyledons Fd-GOGAT is the major form of GOGAT involved in nitrogen assimilation, NADH-GOGAT may be a rate-limiting step in NH4+ assimilation in root nodules Medicago sativa glutamate + NAD+
-
 ?

Subunits

Subunits Comment Organism
monomer
-
 Medicago sativa
More protein contains domains that correspond to both the large alpha subunit with 46% identity and the small beta subunit with 38% identity of Escherichia coli NADPH-GOGAT, a 57 amino acid highly charged domain connects the two regions homologous to the prokaryotic subunits Medicago sativa

Cofactor

Cofactor Comment Organism Structure
flavin iron-sulfur flavoprotein Medicago sativa
FMN coding region important for binding of flavin mononucleotide is located on exon 16 Medicago sativa
NADH five conserved residues important for NADH binding are located in exon 20 Medicago sativa