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Literature summary for 2.6.1.1 extracted from

  • El Omari, R.; Ben Mrid, R.; Bouargalne, Y.; Nhiri, M.
    Prokaryotic-type aspartate aminotransferase in Sorghum leaves localization, distribution and potential role (2020), Russ. J. Plant Physiol., 67, 697-702 .
No PubMed abstract available
Search for more literature for 2.6.1.1

Localization

Localization Comment Organism GeneOntology No. Textmining
plastid
-
 Sorghum bicolor subsp. drummondii 9536
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + 2-oxoglutarate Sorghum bicolor subsp. drummondii
-
 oxaloacetate + L-glutamate
-
 r

Organism

Organism UniProt Comment Textmining
Sorghum bicolor subsp. drummondii
-
 Sudan grass
-

Source Tissue

Source Tissue Comment Organism Textmining
bundle sheath cell
-
 Sorghum bicolor subsp. drummondii
-
leaf
-
 Sorghum bicolor subsp. drummondii
-
mesophyll cell
-
 Sorghum bicolor subsp. drummondii
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
 Sorghum bicolor subsp. drummondii oxaloacetate + L-glutamate
-
 r

Subunits

Subunits Comment Organism
? x * 45000, SDS-PAGE Sorghum bicolor subsp. drummondii

Synonyms

Synonyms Comment Organism
AAT
-
 Sorghum bicolor subsp. drummondii
aspartate aminotransferase
-
 Sorghum bicolor subsp. drummondii
PT-AAT the bifunctional enzyme is implicated not only in the aspartate aminotransferase activity but also characterized by a prephenate aminotransferase activity Sorghum bicolor subsp. drummondii