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Information on EC 1.1.1.B67 - hyoscyamine dehydrogenase
for references in articles please use BRENDA:EC1.1.1.B67
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preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.B67 hyoscyamine dehydrogenase
The expected taxonomic range for this enzyme is: Atropa belladonna
showSynonyms
AbHDH, HDH, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hyoscyamine + NADP+ = hyoscyamine aldehyde + NADPH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
hyoscyamine:NADP+ oxidoreductase
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hyoscyamine + NADP+
hyoscyamine aldehyde + NADPH + H+
Substrates: -
Products: -
Products: -
r
hyoscyamine aldehyde + NADPH + H+
hyoscyamine + NAD+
Substrates: the enzyme is involved in the formation of hyoscyamine
Products: -
Products: -
r
hyoscyamine aldehyde + NADPH + H+
hyoscyamine + NADP+
Substrates: -
Products: -
Products: -
r
phenylacetaldehyde + NADPH + H+
phenylethanol + NADP+
Substrates: no activity when phenylethanol serves as the substrate
Products: -
Products: -
ir
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hyoscyamine aldehyde + NADPH + H+
hyoscyamine + NAD+
Substrates: the enzyme is involved in the formation of hyoscyamine
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
pro-R hydride of NADPH being used for the reduction reaction
NADPH
pro-R hydride of NADPH being used for the reduction reaction
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
the catalytic Zn2+ is coordinated by one histidine (His74), one glutamate (Glu75), and two cysteines (Cys52 and Cys168) and together showing approximate tetrahedral symmetry
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2 - 9
pH 5.2: about 50% of maximal activity, pH 9.0: about 50% of maximal activity, phenyl acetaldehyde as substrate
9 - 11
pH 9.0: about 50% of maximal activity, pH 11.0: about 40% of maximal activity, hyoscyamine as substrate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
25°C: about 60% of maximal activity, 45°C: about 90% of maximal activity, phenyl acetaldehyde as substrate
25 - 50
25°C: about 60% of maximal activity, 50°C: about 20% of maximal activity, hyoscyamine as substrate
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
highly expressed in the secondary roots, moderately expressed in the primary roots
brenda
additional information
not expressed in the stems or leaves
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
suppression of AbHDH using RNAi technology does not reduce the production of hyoscyamine, anisodamine, or scopolamine, though it does increase the accumulation of hyoscyamine aldehyde
physiological function
the enzyme is involved in the formation of hyoscyamine
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 20°C. Crystal structure at a 2.4 A resolution is determined
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C100F
0.16% of the wild-type activity for phenylacetaldehyde and 0.27% of the wild-type activity for hyoscyamine
C100G
enzyme activity profiles of C100G shows 0.70% of the wild-type activity for phenylacetaldehyde and 30.90% of the wild-type activity for hyoscyamine
C100Y
0.16% of the wild-type activity for phenylacetaldehyde and 0.27% of the wild-type activity for hyoscyamine
H74A
mutation leads to loss of enzyme activity for each of the two tested substrates
S54A
the mutant enzyme displays no catalytic activity at all when using phenylacetaldehyde as the substrate. When hyoscyamine is used as the substrate, its activity amounts to just 0.91% of that of the wild type
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
the enzyme is of value in engineering the production of pharmaceutical tropane alkaloids in planta through an overexpression strategy
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Qiu, F.; Yan, Y.; Zeng, J.; Huang, J.-P.; Zeng,L.; Zhong, W.; Lan, X.; Chen, M.; Huang, S.-X.; Liao, Z.
Biochemical metabolic insights into hyoscyamine dehydrogenase
ACS Catal.
11
2912-2924
2021
Atropa belladonna (A0A8A5L0G9)
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.B67)
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Release 2026.1 (March 2026)
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