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Literature summary for 1.5.1.44 extracted from

  • Gerhards, N.; Li, S.M.
    A bifunctional old yellow enzyme from Penicillium roqueforti is involved in ergot alkaloid biosynthesis (2017), Org. Biomol. Chem., 15, 8059-8071 .
    View publication on PubMed

Activating Compound

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(Commentary)

Cloned (Comment) Organism
gene fgaFS, cloning and recombinant expression of His-tagged enzyme in Escherichia coli Penicillium camemberti

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
122900
-
recombinant His-tagged enzyme, gel filtration Penicillium camemberti

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Penicillium camemberti
-
-
-
Penicillium camemberti DSM 1233
-
-
-
Penicillium commune I6U936
-
-
Penicillium roqueforti W6QRI9
-
-
Penicillium roqueforti FM164 W6QRI9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli Penicillium camemberti

Substrates and Products (Substrate)

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

Subunits Comment Organism
tetramer 4 * 28300, recombinant His-tagged enzyme, SDS-PAGE Penicillium camemberti

Synonyms

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Penicillium camemberti
30
-
assay at Penicillium commune
30
-
assay at Penicillium roqueforti

pH Optimum

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

Cofactor Comment Organism Structure
NADH
-
Penicillium camemberti
NADH
-
Penicillium commune
NADH
-
Penicillium roqueforti