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Literature summary extracted from

  • 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 (2012), RSC Adv., 2, 3662-3669.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.44 expressed in Escherichia coli XL1 Blue MRF cells Aspergillus fumigatus
1.5.1.44 expressed in Escherichia coli XL1 Blue MRF cells Penicillium commune

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.44 30000
-
 1 * 30000, His6-tagged enzyme, SDS-PAGe Aspergillus fumigatus
1.5.1.44 30000
-
 1 * 30000, His6-tagged enzyme, SDS-PAGe Penicillium commune
1.5.1.44 32600
-
 1 * 32600, His6-tagged enzyme, calculated from amino acid sequence Aspergillus fumigatus
1.5.1.44 32600
-
 1 * 32600, His6-tagged enzyme, calculated from amino acid sequence Penicillium commune

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.44 Aspergillus fumigatus
-
-
-
1.5.1.44 Aspergillus fumigatus Af293
-
-
-
1.5.1.44 Claviceps purpurea
-
-
-
1.5.1.44 Penicillium commune I6U936
-
-
1.5.1.44 Penicillium commune NRRL2033 I6U936
-
-
1.5.1.46 Claviceps purpurea
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.44 Ni-NTA agarose column chromatography and HisPur Cobalt resin column chromatography Aspergillus fumigatus
1.5.1.44 Ni-NTA agarose column chromatography and HisPur Cobalt resin column chromatography Penicillium commune

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.44 chanoclavine-I aldehyde + NADH + H+ festuclavine synthase FgaFS and the old yellow enzyme FgaOx3 from Aspergillus fumigatus catalyse the formation of festuclavine by two reduction steps Aspergillus fumigatus festuclavine + NAD+
-
 ?
1.5.1.44 chanoclavine-I aldehyde + NADH + H+ festuclavine synthase FgaFS and the old yellow enzyme FgaOx3 from Aspergillus fumigatus catalyse the formation of festuclavine by two reduction steps Penicillium commune festuclavine + NAD+
-
 ?
1.5.1.44 chanoclavine-I aldehyde + NADH + H+ festuclavine synthase FgaFS and the old yellow enzyme FgaOx3 from Aspergillus fumigatus catalyse the formation of festuclavine by two reduction steps Aspergillus fumigatus Af293 festuclavine + NAD+
-
 ?
1.5.1.44 chanoclavine-I aldehyde + NADH + H+ festuclavine synthase FgaFS and the old yellow enzyme FgaOx3 from Aspergillus fumigatus catalyse the formation of festuclavine by two reduction steps Penicillium commune NRRL2033 festuclavine + NAD+
-
 ?
1.5.1.44 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 Claviceps purpurea ?
-
 ?
1.5.1.46 chanoclavine-I aldehyde + GSH + NADPH + H+ the reaction occurs only in the presence of reduced glutathione Claviceps purpurea agroclavine + GSSG + NADP+
-
 ?
1.5.1.46 chanoclavine-I aldehyde + NADPH + H+
-
 Claviceps purpurea festuclavine + pyroclavine + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.44 monomer 1 * 30000, His6-tagged enzyme, SDS-PAGe Aspergillus fumigatus
1.5.1.44 monomer 1 * 30000, His6-tagged enzyme, SDS-PAGe Penicillium commune
1.5.1.44 monomer 1 * 32600, His6-tagged enzyme, calculated from amino acid sequence Aspergillus fumigatus
1.5.1.44 monomer 1 * 32600, His6-tagged enzyme, calculated from amino acid sequence Penicillium commune

Synonyms

EC Number Synonyms Comment Organism
1.5.1.44 EasG
-
 Claviceps purpurea
1.5.1.44 festuclavine synthase
-
 Aspergillus fumigatus
1.5.1.44 festuclavine synthase
-
 Penicillium commune
1.5.1.44 FgaFS
-
 Aspergillus fumigatus
1.5.1.44 FgaFS
-
 Penicillium commune
1.5.1.46 agroclavine synthase
-
 Claviceps purpurea
1.5.1.46 EasG
-
 Claviceps purpurea

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.46 FMN
-
 Claviceps purpurea
1.5.1.46 NADPH NADPH is a better electron donor than NADH Claviceps purpurea