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Literature summary for 2.1.2.13 extracted from

  • Gatzeva-Topalova, P.Z.; May, A.P.; Sousa, M.C.
    Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. (2005), Structure, 13, 929-942.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, crystal structure of the full-length bifunctional ArnA with UDP-glucuronic acid and ATP bound to the dehydrogenase domain. Binding of UDP-glucuronic acid triggers a 17 A conformational change in ArnA_DH that opens the NAD+ binding site while trapping UDP-glucuronic acid Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P77398
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Purification (Commentary)

Purification (Comment) Organism
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Escherichia coli