Information on EC 2.6.1.1 - aspartate transaminase and Organism(s) Drosophila melanogaster

for references in articles please use BRENDA:EC2.6.1.1
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This record set is specific for:
Drosophila melanogaster


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.6.1.1
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RECOMMENDED NAME
GeneOntology No.
aspartate transaminase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(R)-cysteate degradation
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anaerobic energy metabolism (invertebrates, cytosol)
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C4 photosynthetic carbon assimilation cycle, NAD-ME type
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C4 photosynthetic carbon assimilation cycle, PEPCK type
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coenzyme M biosynthesis II
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L-asparagine degradation III (mammalian)
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L-aspartate biosynthesis
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L-aspartate degradation I
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L-aspartate degradation II
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L-glutamate degradation II
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L-phenylalanine degradation IV (mammalian, via side chain)
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partial TCA cycle (obligate autotrophs)
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sulfolactate degradation III
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aspartate and asparagine metabolism
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C4 and CAM-carbon fixation
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coenzyme M biosynthesis
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cysteine metabolism
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gluconeogenesis
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glutamate and glutamine metabolism
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Arginine biosynthesis
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Alanine, aspartate and glutamate metabolism
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Cysteine and methionine metabolism
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Arginine and proline metabolism
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Tyrosine metabolism
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Phenylalanine metabolism
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Phenylalanine, tyrosine and tryptophan biosynthesis
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Novobiocin biosynthesis
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Carbon fixation in photosynthetic organisms
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Isoquinoline alkaloid biosynthesis
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Tropane, piperidine and pyridine alkaloid biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis [7], some EC 2.6.1.57 activity can be found in this enzyme from other sources [8]; indeed the enzymes are identical in Trichomonas vaginalis [6].
CAS REGISTRY NUMBER
COMMENTARY hide
9000-97-9
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