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Literature summary for 1.1.1.195 extracted from

  • Seo, K.H.; Zhuang, N.; Chen, C.; Song, J.Y.; Kang, H.L.; Rhee, K.H.; Lee, K.H.
    Unusual NADPH conformation in the crystal structure of a cinnamyl alcohol dehydrogenase from Helicobacter pylori in complex with NADP(H) and substrate docking analysis (2012), FEBS Lett., 586, 337-343.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Helicobacter pylori

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with NADP(H), to 2.18 A resolution. NADP(H) is bound through hydrophobic interactions within the well-conserved GXGGXG motif from residues Gly184 to Gly189 and the adenine ring is the syn-conformation and is sandwiched between the guanidino group of Arg208 and Thr244 side chains. The aromatic side chains of residues Phe114 and Tyr116 in the active site could bind aromatic aldehydes by stacking the aromatic head of the substrates Helicobacter pylori

Organism

Organism UniProt Comment Textmining
Helicobacter pylori D0ITF8 putative
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