Activating Compound | Comment | Organism | Structure |
---|---|---|---|
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 | Penicillium camemberti | |
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 | Penicillium commune | |
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 | Penicillium roqueforti |
Cloned (Comment) | Organism |
---|---|
gene fgaFS, cloning and recombinant expression of His-tagged enzyme in Escherichia coli | Penicillium camemberti |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
122900 | - |
recombinant His-tagged enzyme, gel filtration | Penicillium camemberti |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | Penicillium camemberti | - |
festuclavine + NAD+ | - |
? | |
6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | Penicillium commune | - |
festuclavine + NAD+ | - |
? | |
6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | Penicillium roqueforti | - |
festuclavine + NAD+ | - |
? | |
6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | Penicillium roqueforti FM164 | - |
festuclavine + NAD+ | - |
? | |
6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | Penicillium camemberti DSM 1233 | - |
festuclavine + NAD+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Penicillium camemberti | - |
- |
- |
Penicillium camemberti DSM 1233 | - |
- |
- |
Penicillium commune | I6U936 | - |
- |
Penicillium roqueforti | W6QRI9 | - |
- |
Penicillium roqueforti FM164 | W6QRI9 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli | Penicillium camemberti |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | - |
Penicillium camemberti | festuclavine + NAD+ | - |
? | |
6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | - |
Penicillium commune | festuclavine + NAD+ | - |
? | |
6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | - |
Penicillium roqueforti | festuclavine + NAD+ | - |
? | |
6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | - |
Penicillium roqueforti FM164 | festuclavine + NAD+ | - |
? | |
6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | - |
Penicillium camemberti DSM 1233 | festuclavine + NAD+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | 4 * 28300, recombinant His-tagged enzyme, SDS-PAGE | Penicillium camemberti |
Synonyms | Comment | Organism |
---|---|---|
festuclavine synthase | - |
Penicillium camemberti |
festuclavine synthase | - |
Penicillium commune |
festuclavine synthase | - |
Penicillium roqueforti |
FgaFS | - |
Penicillium camemberti |
FgaFS | - |
Penicillium commune |
FgaFS | - |
Penicillium roqueforti |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Penicillium camemberti |
30 | - |
assay at | Penicillium commune |
30 | - |
assay at | Penicillium roqueforti |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Penicillium camemberti |
7.5 | - |
assay at | Penicillium commune |
7.5 | - |
assay at | Penicillium roqueforti |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Penicillium camemberti | |
NADH | - |
Penicillium commune | |
NADH | - |
Penicillium roqueforti |