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Information on EC 1.5.1.44 - festuclavine dehydrogenase
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1.5.1.44 festuclavine dehydrogenaseIUBMB Comments
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.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
fgafs, festuclavine synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EasG
ergot alkaloid biosynthetic protein G
festuclavine synthase
festuclavine synthase I
festuclavine synthase II
FgaFS
ifgF1
ifgF2
isofumigaclavine biosynthesis cluster A protein F1
isofumigaclavine biosynthesis cluster A protein F2
festuclavine synthase
-
-
-
-
FgaFS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
festuclavine + NAD+ = 6,8-dimethyl-6,7-didehydroergoline + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
festuclavine + NAD+
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
-
-
-
-
r
additional information
?
-
-
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
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
-
r
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
Aspergillus fumigatus CBS 101355
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
Aspergillus fumigatus FGSC A1100
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
Penicillium camemberti DSM 1233
-
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
chanoclavine-I aldehyde + NADH + H+
festuclavine + NAD+
-
festuclavine synthase FgaFS and the old yellow enzyme FgaOx3 from Aspergillus fumigatus catalyse the formation of festuclavine by two reduction steps
-
-
?
chanoclavine-I aldehyde + NADH + H+
festuclavine + NAD+
-
the reaction occurs in the presence of the old yellow enzyme FgaOx3
-
-
?
chanoclavine-I aldehyde + NADH + H+
festuclavine + NAD+
-
this reaction occurs in the presence of the old yellow enzyme FgaOx3. Together with GSH and NADPH, the enzyme also catalyses the conversion of chanoclavine-I aldehyde to agroclavine in the absence of the old yellow enzyme FgaOx3
-
-
?
chanoclavine-I aldehyde + NADH + H+
festuclavine + NAD+
-
the reaction occurs in the presence of the old yellow enzyme FgaOx3
-
-
?
chanoclavine-I aldehyde + NADH + H+
festuclavine + NAD+
-
festuclavine synthase FgaFS and the old yellow enzyme FgaOx3 from Aspergillus fumigatus catalyse the formation of festuclavine by two reduction steps
-
-
?
chanoclavine-I aldehyde + NADH + H+
festuclavine + NAD+
festuclavine synthase FgaFS and the old yellow enzyme FgaOx3 from Aspergillus fumigatus catalyse the formation of festuclavine by two reduction steps
-
-
?
chanoclavine-I aldehyde + NADH + H+
festuclavine + NAD+
festuclavine synthase FgaFS and the old yellow enzyme FgaOx3 from Aspergillus fumigatus catalyse the formation of festuclavine by two reduction steps
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
Aspergillus fumigatus CBS 101355
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
Aspergillus fumigatus FGSC A1100
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
Penicillium camemberti DSM 1233
-
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
6,8-dimethyl-6,7-didehydroergoline + NADH + H+
festuclavine + NAD+
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FgaOx3Pr3
-
the enzyme shows high homology to old yellow enzymes (OYEs) involved in the ergot alkaloid biosynthesis, but it is found outside the two clusters. Biochemical characterisation of this enzyme, named FgaOx3Pr3, shows that it can indeed catalyse the formation of festuclavine in the presence of a festuclavine synthase FgaFS, as had been observed for other OYEs in ergot alkaloid biosynthesis. It works as a reaction enhancer with festuclavine synthase (EasG, festuclavine dehydrogenase) and chanoclavine-I dehydrogenase (ChaDH). FgaOx3Pr3 is a better reaction partner for agroclavine synthase EasG than glutahione (GSH). Identification of an additional OYE homologue, FgaOx3Pr3. This unique OYE not only fulfils the same function as its orthologues from Aspergillus fumigatus and Penicillium commune in the formation of festuclavine but it also enhances the enzyme activities of several SDRs for the conversion of 1 to 2 tremendously. Kinetic studies reveal that this enhancement is contributes by reduction of the product inhibition postulated for the chanoclavine-I dehydrogenase
-
FgaOx3Pr3
the enzyme shows high homology to old yellow enzymes (OYEs) involved in the ergot alkaloid biosynthesis, but it is found outside the two clusters. Biochemical characterisation of this enzyme, named FgaOx3Pr3, shows that it can indeed catalyse the formation of festuclavine in the presence of a festuclavine synthase FgaFS, as had been observed for other OYEs in ergot alkaloid biosynthesis. It works as a reaction enhancer with festuclavine synthase (EasG, festuclavine dehydrogenase) and chanoclavine-I dehydrogenase (ChaDH). FgaOx3Pr3 is a better reaction partner for agroclavine synthase EasG than glutahione (GSH). Identification of an additional OYE homologue, FgaOx3Pr3. This unique OYE not only fulfils the same function as its orthologues from Aspergillus fumigatus and Penicillium commune in the formation of festuclavine but it also enhances the enzyme activities of several SDRs for the conversion of 1 to 2 tremendously. Kinetic studies reveal that this enhancement is contributes by reduction of the product inhibition postulated for the chanoclavine-I dehydrogenase
-
FgaOx3Pr3
the enzyme shows high homology to old yellow enzymes (OYEs) involved in the ergot alkaloid biosynthesis, but it is found outside the two clusters. Biochemical characterisation of this enzyme, named FgaOx3Pr3, shows that it can indeed catalyse the formation of festuclavine in the presence of a festuclavine synthase FgaFS, as had been observed for other OYEs in ergot alkaloid biosynthesis. It works as a reaction enhancer with festuclavine synthase (EasG, festuclavine dehydrogenase) and chanoclavine-I dehydrogenase (ChaDH). FgaOx3Pr3 is a better reaction partner for agroclavine synthase EasG than glutahione (GSH). Identification of an additional OYE homologue, FgaOx3Pr3. This unique OYE not only fulfils the same function as its orthologues from Aspergillus fumigatus and Penicillium commune in the formation of festuclavine but it also enhances the enzyme activities of several SDRs for the conversion of 1 to 2 tremendously. Kinetic studies reveal that this enhancement is contributes by reduction of the product inhibition postulated for the chanoclavine-I dehydrogenase
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
organization of the clavine gene clusters in different species, e.g. clusters A and B of isofumigaclavine in Penicillium roqueforti, overview
evolution
organization of the clavine gene clusters in different species, e.g. fumigaclavine A gene cluster of Penicillium commune, overview
evolution
organization of the clavine gene clusters in different species, e.g. fumigaclavine C gene cluster in Neosartorya fumigata, overview
evolution
-
organization of the clavine gene clusters in different species, overview
evolution
-
organization of the clavine gene clusters in different species, e.g. clusters A and B of isofumigaclavine in Penicillium roqueforti, overview
-
evolution
Aspergillus fumigatus CBS 101355
-
organization of the clavine gene clusters in different species, e.g. fumigaclavine C gene cluster in Neosartorya fumigata, overview
-
evolution
-
organization of the clavine gene clusters in different species, e.g. fumigaclavine C gene cluster in Neosartorya fumigata, overview
-
evolution
Aspergillus fumigatus FGSC A1100
-
organization of the clavine gene clusters in different species, e.g. fumigaclavine C gene cluster in Neosartorya fumigata, overview
-
evolution
-
organization of the clavine gene clusters in different species, e.g. fumigaclavine C gene cluster in Neosartorya fumigata, overview
-
malfunction
accumulation of prenylated intermediates and lack of fumigaclavine A formation has been reported in mutants of Neosartorya fumigata disrupted in the festuclavine hydroxylase
malfunction
Aspergillus fumigatus CBS 101355
-
accumulation of prenylated intermediates and lack of fumigaclavine A formation has been reported in mutants of Neosartorya fumigata disrupted in the festuclavine hydroxylase
-
malfunction
-
accumulation of prenylated intermediates and lack of fumigaclavine A formation has been reported in mutants of Neosartorya fumigata disrupted in the festuclavine hydroxylase
-
malfunction
Aspergillus fumigatus FGSC A1100
-
accumulation of prenylated intermediates and lack of fumigaclavine A formation has been reported in mutants of Neosartorya fumigata disrupted in the festuclavine hydroxylase
-
malfunction
-
accumulation of prenylated intermediates and lack of fumigaclavine A formation has been reported in mutants of Neosartorya fumigata disrupted in the festuclavine hydroxylase
-
metabolism
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A. Comparison of the synthetic pathway of isofumigaclavine A in Penicillium roqueforti and fumigaclavine C in Neosartorya fumigata
metabolism
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A. Finally, in Neosartorya fumigata, there is a step that involves the prenylation of fumigaclavine A to form fumigaclavine C. Comparison of the synthetic pathway of isofumigaclavine A in Penicillium roqueforti and fumigaclavine C in Neosartorya fumigata
metabolism
-
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A
metabolism
-
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A
metabolism
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A
metabolism
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A
metabolism
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A
metabolism
-
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A. Comparison of the synthetic pathway of isofumigaclavine A in Penicillium roqueforti and fumigaclavine C in Neosartorya fumigata
-
metabolism
Aspergillus fumigatus CBS 101355
-
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A. Finally, in Neosartorya fumigata, there is a step that involves the prenylation of fumigaclavine A to form fumigaclavine C. Comparison of the synthetic pathway of isofumigaclavine A in Penicillium roqueforti and fumigaclavine C in Neosartorya fumigata
-
metabolism
-
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A. Finally, in Neosartorya fumigata, there is a step that involves the prenylation of fumigaclavine A to form fumigaclavine C. Comparison of the synthetic pathway of isofumigaclavine A in Penicillium roqueforti and fumigaclavine C in Neosartorya fumigata
-
metabolism
Aspergillus fumigatus FGSC A1100
-
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A. Finally, in Neosartorya fumigata, there is a step that involves the prenylation of fumigaclavine A to form fumigaclavine C. Comparison of the synthetic pathway of isofumigaclavine A in Penicillium roqueforti and fumigaclavine C in Neosartorya fumigata
-
metabolism
-
clavine and lysergic acid-containing alkaloids derive from the condensation of tryptophan and dimethylallylpyrophosphate (DMA-PP), catalyzed by the first enzyme of the pathway, named dimethylallyltryptophan synthase (DMATS). This results in the formation of tricyclic intermediates, the most relevant being chanoclavine I and chanoclavine I aldehyde, which the branch point intermediate for the formation of different types of alkaloids. Chanoclavine I aldehyde, is later cyclized to form the tetracyclic ergoline nucleus. The ergoline structure constitutes the nucleus of festuclavine, agroclavine, elymoclavine, pyroclavine and their derivatives. In agroclavine and elymoclavine, there is a double bond between carbons C-8 and C-9, whereas in festuclavine this double bond is not present. Pyroclavine, an C-8 stereoisomer (carbons 8R/9S) of festuclavine (carbon 8S/9S), is also present in cultures of some of the clavine alkaloids producers. The late steps of the biosynthesis of fumigaclavine alkaloids involve the oxidation of festuclavine to 9-hydroxyfestuclavine (named fumigaclavine B) and later the acetylation of fumigaclavine B to fumigaclavine A. Finally, in Neosartorya fumigata, there is a step that involves the prenylation of fumigaclavine A to form fumigaclavine C. Comparison of the synthetic pathway of isofumigaclavine A in Penicillium roqueforti and fumigaclavine C in Neosartorya fumigata
-
physiological function
gene ifgF1 encodes a festuclavine synthase that is involved in the conversion of chanoclavine I aldehyde into festuclavine
physiological function
-
gene ifgF1 encodes a festuclavine synthase that is involved in the conversion of chanoclavine I aldehyde into festuclavine
-
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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). IFGF1_PENRF
Penicillium roqueforti (strain FM164)
287
0
31612
Swiss-Prot
Mitochondrion (Reliability: 4)
IFGF2_PENRF
Penicillium roqueforti (strain FM164)
287
0
31416
Swiss-Prot
Mitochondrion (Reliability: 3)
EASG_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
290
0
32109
Swiss-Prot
Mitochondrion (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
32600
32600
-
1 * 32600, His6-tagged enzyme, calculated from amino acid sequence
32600
1 * 32600, His6-tagged enzyme, calculated from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
tetramer
monomer
-
1 * 32600, His6-tagged enzyme, calculated from amino acid sequence
monomer
-
1 * 32600, His6-tagged enzyme, calculated from amino acid sequence
-
monomer
1 * 32600, His6-tagged enzyme, calculated from amino acid sequence
monomer
-
1 * 32600, His6-tagged enzyme, calculated from amino acid sequence
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y178F
-
the activity of the mutant is not qualitatively different from wild type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography and HisPur Cobalt resin column chromatography
Ni-NTA agarose column chromatography and HisPur Cobalt resin column chromatography
-
Ni-NTA agarose column chromatography and HisPur Cobalt resin column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL1 Blue MRF cells
gene fgaFS, cloning and recombinant expression of His-tagged enzyme in Escherichia coli
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheng, J.; Coyle, C.; Panaccione, D.; OConnor, S.
Controlling a structural branch point in ergot alkaloid biosynthesis
J. Am. Chem. Soc.
132
12835-12837
2010
Aspergillus fumigatus
brenda
Xie, X.; Wallwey, C.; Matuschek, M.; Steinbach, K.; Li, S.M.
Formyl migration product of chanoclavine-I aldehyde in the presence of the old yellow enzyme FgaOx3 from Aspergillus fumigatus: a NMR structure elucidation
Magn. Reson. Chem.
49
678-681
2011
Aspergillus fumigatus
brenda
Wallwey, C.; Matuschek, M.; Xie, X.; Li, S.
Ergot alkaloid biosynthesis in Aspergillus fumigatus: Conversion of chanoclavine-I aldehyde to festuclavine by the festuclavine synthase FgaFS in the presence of the old yellow enzyme FgaOx3
Org. Biomol. Chem.
8
3500-3508
2010
Aspergillus fumigatus, Aspergillus fumigatus Af293
brenda
Matuschek, M.; Wallwey, C.; Xie, X.; Li, S.M.
New insights into ergot alkaloid biosynthesis in Claviceps purpurea: an agroclavine synthase EasG catalyses, via a non-enzymatic adduct with reduced glutathione, the conversion of chanoclavine-I aldehyde to agroclavine
Org. Biomol. Chem.
9
4328-4335
2011
Aspergillus fumigatus
brenda
Matuschek, M.; Wallwey, C.; Wollinsky, B.; Xie, X.; Li, S.
In vitro conversion of chanoclavine-I aldehyde to the stereoisomers festuclavine and pyroclavine controlled by the second reduction step
RSC Adv.
2
3662-3669
2012
Aspergillus fumigatus, Claviceps purpurea, Penicillium commune (I6U936), Aspergillus fumigatus Af293, Penicillium commune NRRL2033 (I6U936)
-
brenda
Gerhards, N.; Li, S.M.
A bifunctional old yellow enzyme from Penicillium roqueforti is involved in ergot alkaloid biosynthesis
Org. Biomol. Chem.
15
8059-8071
2017
Penicillium camemberti, Penicillium commune (I6U936), Penicillium roqueforti (W6QRI9), Penicillium roqueforti, Penicillium roqueforti FM164 (W6QRI9), Penicillium camemberti DSM 1233
brenda
Martin, J.F.; Alvarez-Alvarez, R.; Liras, P.
Clavine alkaloids gene clusters of Penicillium and related fungi evolutionary combination of prenyltransferases, monooxygenases and dioxygenases
Genes (Basel)
8
342
2017
Penicillium camemberti, Penicillium griseofulvum, Penicillium expansum (A0A0A2J928), Penicillium steckii (A0A1V6SJK0), Penicillium commune (I6U936), Aspergillus fumigatus (Q4WZ69), Penicillium roqueforti (W6Q1E9), Penicillium roqueforti (W6QRI9), Penicillium roqueforti FM164 (W6Q1E9), Penicillium roqueforti FM164 (W6QRI9), Aspergillus fumigatus CBS 101355 (Q4WZ69), Aspergillus fumigatus ATCC MYA-4609 (Q4WZ69), Aspergillus fumigatus FGSC A1100 (Q4WZ69), Aspergillus fumigatus Af293 (Q4WZ69)
brenda
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Release 2023.1 (January 2023)
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