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Literature summary for 2.6.1.82 extracted from

  • Cha, H.; Jeong, J.; Rojviriya, C.; Kim, Y.
    Structure of putrescine aminotransferase from Escherichia coli provides insights into the substrate specificity among class III aminotransferases (2014), PLoS ONE, 9, e113212.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of YgjG at 2.3 and 2.1 A resolutions for the free and putrescine-bound enzymes, respectively. YgjG forms a dimer that adopts a class III pyridoxal 5'-phosphate-dependent aminotransferase fold. Structures of YgjG and other class III aminotransferases are similar. YgjG has an additional N-terminal helical structure that partially contributes to a dimeric interaction with the other subunit via a helix-helix interaction. The YgjG substrate-binding site entrance size and charge distribution are smaller and more hydrophobic than other class III aminotransferases Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P42588
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Synonyms

Synonyms Comment Organism
PatA
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Escherichia coli
YjgG
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Escherichia coli