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EC Number
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2.6.1.1
Aspartate aminotransferase is potently inhibited by copper complexes Exploring copper complex-binding proteome
Rattus norvegicus
2.6.1.1
Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis
Mycobacterium tuberculosis
2.6.1.1
Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis
Mycobacterium tuberculosis H37Rv
2.6.1.1
Biochemical characterization and structure-based mutational analysis provide insight into the binding and mechanism of action of novel aspartate aminotransferase inhibitors
Homo sapiens
2.6.1.1
Chemoenzymatic synthesis of L-3,4-dimethoxyphenyl-alanine and its analogues using aspartate aminotransferase as a key catalyst
Escherichia coli
2.6.1.1
Conversion of cysteine to 3-mercaptopyruvic acid by bacterial aminotransferases
Cupriavidus necator
2.6.1.1
Conversion of cysteine to 3-mercaptopyruvic acid by bacterial aminotransferases
Shimwellia blattae
2.6.1.1
Conversion of cysteine to 3-mercaptopyruvic acid by bacterial aminotransferases
Escherichia coli
2.6.1.1
Conversion of cysteine to 3-mercaptopyruvic acid by bacterial aminotransferases
Advenella mimigardefordensis
2.6.1.1
Conversion of cysteine to 3-mercaptopyruvic acid by bacterial aminotransferases
Advenella mimigardefordensis DPN7
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