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Literature summary for 1.14.11.11 extracted from

  • Matsuda, J.; Hashimoto, T.; Yamada, Y.
    Analysis of active-site residues in hyoscyamine 6beta-hydroxylase (1997), Plant Biotechnol., 14, 51-57.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli as a fusion protein to maltose-binding protein Hyoscyamus niger

Protein Variants

Protein Variants Comment Organism
D219H inactive mutant enzyme Hyoscyamus niger
D219N inactive mutant enzyme Hyoscyamus niger
H217Q inactive mutant enzyme Hyoscyamus niger
H66Q mutant enzyme has 97% of the activity of the wild-type enzyme Hyoscyamus niger
S274Q inactive mutant enzyme Hyoscyamus niger

Organism

Organism UniProt Comment Textmining
Hyoscyamus niger
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-hyoscyamine + 2-oxoglutarate + O2
-
Hyoscyamus niger 6beta-hydroxyhyoscyamine + succinate + CO2
-
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