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Literature summary extracted from
- A bifunctional old yellow enzyme from Penicillium roqueforti is involved in ergot alkaloid biosynthesis (2017), Org. Biomol. Chem., 15, 8059-8071 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.332 | FgaOx3Pr3 | an old yellow enzyme (OYE), does not convert chanoclavine-I aldehyde to its shunt products in the absence of FgaFS. Instead, it increases significantly the product yields of several SDRs for the conversion of chanoclavine-I to its aldehyde. Kinetic studies prove that overcoming the product inhibition is responsible for the observed enhancement. Bifunctionality of OYE and synergistic effect with SDRs | Penicillium roqueforti | |
| 1.5.1.44 | 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 | |
| 1.5.1.44 | 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 | |
| 1.5.1.44 | 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(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.3.1.100 | expressed in Escherichia coli M15 cells | Penicillium roqueforti |
| 1.5.1.44 | gene fgaFS, cloning and recombinant expression of His-tagged enzyme in Escherichia coli | Penicillium camemberti |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.332 | 0.082 | - |
NAD+ | pH not specified in the publication, 30°C | Penicillium roqueforti |  |
| 1.1.1.332 | 0.573 | - |
chanoclavine-I | pH not specified in the publication, 30°C | Penicillium roqueforti | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.44 | 122900 | - |
recombinant His-tagged enzyme, gel filtration | Penicillium camemberti |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.332 | chanoclavine-I + NAD+ | Penicillium roqueforti | - |
chanoclavine-I aldehyde + NADH + H+ | - |
r | |
| 1.1.1.332 | chanoclavine-I + NAD+ | Penicillium roqueforti FM164 | - |
chanoclavine-I aldehyde + NADH + H+ | - |
r | |
| 1.3.1.100 | chanoclavine-I aldehyde + NADPH + H+ | Aspergillus fumigatus | - |
dihydrochanoclavine-I aldehyde + NADP+ | - |
? | |
| 1.3.1.100 | chanoclavine-I aldehyde + NADPH + H+ | Penicillium roqueforti | - |
dihydrochanoclavine-I aldehyde + NADP+ | - |
? | |
| 1.3.1.100 | chanoclavine-I aldehyde + NADPH + H+ | Penicillium roqueforti FM164 | - |
dihydrochanoclavine-I aldehyde + NADP+ | - |
? | |
| 1.3.1.100 | chanoclavine-I aldehyde + NADPH + H+ | Aspergillus fumigatus ATCC MYA-4609 | - |
dihydrochanoclavine-I aldehyde + NADP+ | - |
? | |
| 1.5.1.44 | 6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | Penicillium camemberti | - |
festuclavine + NAD+ | - |
? | |
| 1.5.1.44 | 6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | Penicillium commune | - |
festuclavine + NAD+ | - |
? | |
| 1.5.1.44 | 6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | Penicillium roqueforti | - |
festuclavine + NAD+ | - |
? | |
| 1.5.1.44 | 6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | Penicillium roqueforti FM164 | - |
festuclavine + NAD+ | - |
? | |
| 1.5.1.44 | 6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | Penicillium camemberti DSM 1233 | - |
festuclavine + NAD+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.332 | Penicillium roqueforti | - |
- |
- |
| 1.1.1.332 | Penicillium roqueforti FM164 | - |
- |
- |
| 1.3.1.100 | Aspergillus fumigatus | Q4WZ70 | - |
- |
| 1.3.1.100 | Aspergillus fumigatus ATCC MYA-4609 | Q4WZ70 | - |
- |
| 1.3.1.100 | no activity in Claviceps purpurea | - |
- |
- |
| 1.3.1.100 | Penicillium roqueforti | W6Q9S9 | - |
- |
| 1.3.1.100 | Penicillium roqueforti FM164 | W6Q9S9 | - |
- |
| 1.5.1.44 | Penicillium camemberti | - |
- |
- |
| 1.5.1.44 | Penicillium camemberti DSM 1233 | - |
- |
- |
| 1.5.1.44 | Penicillium commune | I6U936 | - |
- |
| 1.5.1.44 | Penicillium roqueforti | W6QRI9 | - |
- |
| 1.5.1.44 | Penicillium roqueforti FM164 | W6QRI9 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.3.1.100 | Ni-NTA agarose resin column chromatography | Penicillium roqueforti |
| 1.5.1.44 | recombinant His-tagged enzyme from Escherichia coli | Penicillium camemberti |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.332 | chanoclavine-I + NAD+ | - |
Penicillium roqueforti | chanoclavine-I aldehyde + NADH + H+ | - |
r | |
| 1.1.1.332 | chanoclavine-I + NAD+ | - |
Penicillium roqueforti FM164 | chanoclavine-I aldehyde + NADH + H+ | - |
r | |
| 1.1.1.332 | additional information | LC-MS analysis of the in vitro assays | Penicillium roqueforti | ? | - |
- |
|
| 1.1.1.332 | additional information | LC-MS analysis of the in vitro assays | Penicillium roqueforti FM164 | ? | - |
- |
|
| 1.3.1.100 | chanoclavine-I aldehyde + NADPH + H+ | - |
Aspergillus fumigatus | dihydrochanoclavine-I aldehyde + NADP+ | - |
? | |
| 1.3.1.100 | chanoclavine-I aldehyde + NADPH + H+ | - |
Penicillium roqueforti | dihydrochanoclavine-I aldehyde + NADP+ | - |
? | |
| 1.3.1.100 | chanoclavine-I aldehyde + NADPH + H+ | - |
Penicillium roqueforti FM164 | dihydrochanoclavine-I aldehyde + NADP+ | - |
? | |
| 1.3.1.100 | chanoclavine-I aldehyde + NADPH + H+ | - |
Aspergillus fumigatus ATCC MYA-4609 | dihydrochanoclavine-I aldehyde + NADP+ | - |
? | |
| 1.5.1.44 | 6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | - |
Penicillium camemberti | festuclavine + NAD+ | - |
? | |
| 1.5.1.44 | 6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | - |
Penicillium commune | festuclavine + NAD+ | - |
? | |
| 1.5.1.44 | 6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | - |
Penicillium roqueforti | festuclavine + NAD+ | - |
? | |
| 1.5.1.44 | 6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | - |
Penicillium roqueforti FM164 | festuclavine + NAD+ | - |
? | |
| 1.5.1.44 | 6,8-dimethyl-6,7-didehydroergoline + NADH + H+ | - |
Penicillium camemberti DSM 1233 | festuclavine + NAD+ | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.3.1.100 | ? | x * 45000, His6-tagged enzyme, SDS-PAGE | Penicillium roqueforti |
| 1.5.1.44 | tetramer | 4 * 28300, recombinant His-tagged enzyme, SDS-PAGE | Penicillium camemberti |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.1.332 | ChaDH | - |
Penicillium roqueforti |
| 1.1.1.332 | FgaDHPr | - |
Penicillium roqueforti |
| 1.1.1.332 | ifgE | - |
Penicillium roqueforti |
| 1.3.1.100 | FgaOx3 | - |
Aspergillus fumigatus |
| 1.3.1.100 | FgaOx3Pr3 | - |
Penicillium roqueforti |
| 1.5.1.44 | festuclavine synthase | - |
Penicillium camemberti |
| 1.5.1.44 | festuclavine synthase | - |
Penicillium commune |
| 1.5.1.44 | festuclavine synthase | - |
Penicillium roqueforti |
| 1.5.1.44 | FgaFS | - |
Penicillium camemberti |
| 1.5.1.44 | FgaFS | - |
Penicillium commune |
| 1.5.1.44 | FgaFS | - |
Penicillium roqueforti |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.332 | 30 | - |
assay at | Penicillium roqueforti |
| 1.5.1.44 | 30 | - |
assay at | Penicillium camemberti |
| 1.5.1.44 | 30 | - |
assay at | Penicillium commune |
| 1.5.1.44 | 30 | - |
assay at | Penicillium roqueforti |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.332 | 0.135 | - |
NAD+ | pH not specified in the publication, 30°C | Penicillium roqueforti | |
| 1.1.1.332 | 0.172 | - |
chanoclavine-I | pH not specified in the publication, 30°C | Penicillium roqueforti | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.44 | 7.5 | - |
assay at | Penicillium camemberti |
| 1.5.1.44 | 7.5 | - |
assay at | Penicillium commune |
| 1.5.1.44 | 7.5 | - |
assay at | Penicillium roqueforti |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.332 | NAD+ | - |
Penicillium roqueforti | |
| 1.1.1.332 | NADH | - |
Penicillium roqueforti | |
| 1.3.1.100 | FMN | - |
Aspergillus fumigatus | |
| 1.3.1.100 | FMN | - |
Penicillium roqueforti | |
| 1.3.1.100 | NADPH | - |
Aspergillus fumigatus | |
| 1.3.1.100 | NADPH | - |
Penicillium roqueforti | |
| 1.5.1.44 | NADH | - |
Penicillium camemberti | |
| 1.5.1.44 | NADH | - |
Penicillium commune | |
| 1.5.1.44 | NADH | - |
Penicillium roqueforti | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.1.1.332 | evolution | the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) family | Penicillium roqueforti |
| 1.1.1.332 | metabolism | the enzyme is involved in the biosynthesis of festuclavine from dimethylallylpyrosphosphate and tryptophane, the ergot alkaloid pathway | Penicillium roqueforti |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.332 | 0.3 | - |
chanoclavine-I | pH not specified in the publication, 30°C | Penicillium roqueforti | |
| 1.1.1.332 | 1.65 | - |
NAD+ | pH not specified in the publication, 30°C | Penicillium roqueforti | |
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