Information on EC 1.5.1.44 - festuclavine dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.1.44
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RECOMMENDED NAME
GeneOntology No.
festuclavine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
festuclavine + NAD+ = 6,8-dimethyl-6,7-didehydroergoline + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fumigaclavine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
festuclavine:NAD+ oxidoreductase
The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family. The reaction proceeds in vivo in the opposite direction to the one shown here.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
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
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
show the reaction diagram
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r
chanoclavine-I aldehyde + NADH + H+
festuclavine + NAD+
show the reaction diagram
festuclavine + NAD+
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
show the reaction diagram
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r
additional information
?
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in the absence of reduced glutathione, agroclavine synthase EasG also converts chanoclavine-I aldehyde to pyroclavine and festuclavine in the presence of the old yellow enzyme FgaOx3 and NADPH
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
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Ni-NTA agarose column chromatography and HisPur Cobalt resin column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL1 Blue MRF cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F176Y
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the mutant produces agroclavine from chanoclavine-I aldehyde
Y178F
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the activity of the mutant is not qualitatively different from wild type enzyme