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Literature summary for 1.5.3.6 extracted from

  • Kachalova, G.S.; Bourenkov, G.P.; Mengesdorf, T.; Schenk, S.; Maun, H.R.; Burghammer, M.; Riekel, C.; Decker, K.; Bartunik, H.D.
    Crystal structure analysis of free and substrate-bound 6-hydroxy-L-nicotine oxidase from Arthrobacter nicotinovorans (2010), J. Mol. Biol., 396, 785-799.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Paenarthrobacter nicotinovorans

Crystallization (Commentary)

Crystallization (Comment) Organism
a comparison of the substrate-binding modes of 6-hydroxy-D-nicotine oxidase and 6-hydroxy-L-nicotine oxidase, EC 1.5.3.5, based on models of complexes with the D-substrate, suggests that the two enzymes orient the enantiomeric substrates in mirror symmetry with respect to the plane of the flavin Paenarthrobacter nicotinovorans

Organism

Organism UniProt Comment Textmining
Paenarthrobacter nicotinovorans
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