Information on EC 1.1.1.275 - (+)-trans-carveol dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.275
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RECOMMENDED NAME
GeneOntology No.
(+)-trans-carveol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(+)-trans-carveol + NAD+ = (+)-(S)-carvone + NADH + H+
show the reaction diagram
NADP+ cannot replace NAD+. Forms part of the monoterpenoid biosynthesis pathway in Carum carvi (caraway) seeds.
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(4S)-carveol and (4S)-dihydrocarveol degradation
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(4S)-carvone biosynthesis
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Monoterpenoid biosynthesis
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Limonene and pinene degradation
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
(+)-trans-carveol:NAD+ oxidoreductase
NADP+ cannot replace NAD+. Forms part of the monoterpenoid biosynthesis pathway in Carum carvi (caraway) seeds.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
var. Karzo
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Rhodococcus opacus PWD4 / DSM 44313
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-trans-carveol + NAD+
(+)-carvone + NADH
show the reaction diagram
(-)-cis-carveol + NAD+
(-)-carvone + NADH
show the reaction diagram
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65% activity compared to (+)/(-)-trans-carveol
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?
(-)-trans-carveol + NAD+
?
show the reaction diagram
(-)/(+)-cis-carveol + NAD+
(-)-carvone + NADH
show the reaction diagram
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?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(+)-trans-carveol + NAD+
(+)-carvone + NADH
show the reaction diagram
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enzyme catalyses the final step of (+)-carvone biosynthesis, which is developmentally regulated, key enzyme of the pathway is limonene-6-hydroxylase
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
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about
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
additional information
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developmental regulation, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium avium (strain 104)
A0A0H2ZV91
Mycobacterium avium (strain 104)
Mycobacterium avium (strain 104)
Mycobacterium avium (strain 104)
Mycobacterium avium (strain 104)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.55 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover; to 1.95 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover; to 1.95 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover; to 2.0 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover; to 2.15 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
to 1.85 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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