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Information on EC 1.3.1.100 - chanoclavine-I aldehyde reductase
for references in articles please use BRENDA:EC1.3.1.100
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.1 With NAD+ or NADP+ as acceptor
1.3.1.100 chanoclavine-I aldehyde reductase
IUBMB Comments
Contains FMN. The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family. The enzyme catalyses the reduction of chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde. This hydrolyses spontaneously to form 6,8-dimethyl-6,7-didehydroergoline, which is converted to festuclavine by EC 1.5.1.44, festuclavine dehydrogenase.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
fgaox3, fgaox3pr3, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EasA
FgaOx3
FgaOx3Pr3
old yellow enzyme
EasA
-
-
-
-
FgaOx3
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dihydrochanoclavine-I aldehyde + NADP+ = chanoclavine-I aldehyde + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
fumigaclavine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
chanoclavine-I aldehyde:NAD+ oxidoreductase
Contains FMN. The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family. The enzyme catalyses the reduction of chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde. This hydrolyses spontaneously to form 6,8-dimethyl-6,7-didehydroergoline, which is converted to festuclavine by EC 1.5.1.44, festuclavine dehydrogenase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chanoclavine-I aldehyde + NADH + H+
dihydrochanoclavine-I aldehyde + NAD+
Substrates: -
Products: -
Products: -
?
chanoclavine-I aldehyde + NADH + H+
dihydrochanoclavine-I aldehyde + NAD+
Substrates: in the presence of FgaFS only
Products: -
Products: -
?
chanoclavine-I aldehyde + NADH + H+
dihydrochanoclavine-I aldehyde + NAD+
Substrates: in the presence of FgaFS only
Products: -
Products: -
?
chanoclavine-I aldehyde + NADPH + H+
dihydrochanoclavine-I aldehyde + NADP+
-
Substrates: -
Products: -
Products: -
?
chanoclavine-I aldehyde + NADPH + H+
dihydrochanoclavine-I aldehyde + NADP+
Substrates: -
Products: -
Products: -
?
chanoclavine-I aldehyde + NADPH + H+
dihydrochanoclavine-I aldehyde + NADP+
Substrates: -
Products: -
Products: -
?
chanoclavine-I aldehyde + NADPH + H+
dihydrochanoclavine-I aldehyde + NADP+
Substrates: -
Products: -
Products: -
?
chanoclavine-I aldehyde + NADPH + H+
dihydrochanoclavine-I aldehyde + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is more active in the presence of FMN and NADH than other combinations, e.g. FMN and NADPH, FAD and NADH or FAD and NADPH
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is more active in the presence of FMN and NADH than other combinations, e.g. FMN and NADPH, FAD and NADH or FAD and NADPH
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is more active in the presence of FMN and NADH than other combinations, e.g. FMN and NADPH, FAD and NADH or FAD and NADPH
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chanoclavine-I aldehyde + NADH + H+
dihydrochanoclavine-I aldehyde + NAD+
Substrates: -
Products: -
Products: -
?
chanoclavine-I aldehyde + NADPH + H+
dihydrochanoclavine-I aldehyde + NADP+
Substrates: -
Products: -
Products: -
?
chanoclavine-I aldehyde + NADPH + H+
dihydrochanoclavine-I aldehyde + NADP+
Substrates: -
Products: -
Products: -
?
chanoclavine-I aldehyde + NADPH + H+
dihydrochanoclavine-I aldehyde + NADP+
Substrates: -
Products: -
Products: -
?
chanoclavine-I aldehyde + NADPH + H+
dihydrochanoclavine-I aldehyde + NADP+
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.048
chanoclavine-I aldehyde
-
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
38.5
chanoclavine-I aldehyde
-
pH and temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
malfunction
-
disruption of the easA gene leads to accumulation of chanoclavine-I and chanoclavine-I-aldehyde
malfunction
-
disruption of the easA gene leads to accumulation of chanoclavine-I and chanoclavine-I-aldehyde
-
metabolism
-
the enzyme is required for incorporation of chanoclavine-I-aldehyde into more-complex ergot alkaloids, presumably by reducing the double bond conjugated to the aldehyde group, thus facilitating ring closure
metabolism
-
the enzyme is required for incorporation of chanoclavine-I-aldehyde into more-complex ergot alkaloids, presumably by reducing the double bond conjugated to the aldehyde group, thus facilitating ring closure
-
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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). IFGG_PENRF
Penicillium roqueforti (strain FM164)
375
0
41775
Swiss-Prot
other Location (Reliability: 5)
EASA_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
376
0
42186
Swiss-Prot
other Location (Reliability: 4)
FGOX3_PENRF
Penicillium roqueforti (strain FM164)
369
0
40053
Swiss-Prot
Mitochondrion (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.8 A resolution. EasA is a strong structural homolog of old yellow enzyme OYE. The structure is a classic alpha/beta-barrel built up by consecutive alpha/beta motifs to form a central eight-stranded parallel beta-barrel surrounded by alpha-helices. The N-terminus forms a short antiparallel two-stranded beta-sheet that closes off the back of the barrel. The FMN is bound at the other end of the barrel
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q4WZ70), 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 (V5IVA1), Aspergillus fumigatus, Aspergillus fumigatus B5233 (V5IVA1)
brenda
Coyle, C.M.; Cheng, J.Z.; OConnor, S.E.; Panaccione, D.G.
An old yellow enzyme gene controls the branch point between Aspergillus fumigatus and Claviceps purpurea ergot alkaloid pathways
Appl. Environ. Microbiol.
76
3898-3903
2010
Aspergillus fumigatus, Aspergillus fumigatus FGSC A1141
brenda
Cheng, J.; Coyle, C.; Panaccione, D.; O'Connor, S.
A role for old yellow enzyme in ergot alkaloid biosynthesis
J. Am. Chem. Soc.
132
1776-1777
2010
Aspergillus fumigatus
brenda
Chilton, A.S.; Ellis, A.L.; Lamb, A.L.
Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis
Acta Crystallogr. Sect. F
70
1328-1332
2014
Aspergillus fumigatus (Q4WZ70), Aspergillus fumigatus ATCC MYA-4609 (Q4WZ70)
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
Aspergillus fumigatus (Q4WZ70), Aspergillus fumigatus ATCC MYA-4609 (Q4WZ70), no activity in Claviceps purpurea, Penicillium roqueforti (W6Q9S9), Penicillium roqueforti, Penicillium roqueforti FM164 (W6Q9S9)
brenda
EXTERNAL LINKS (specific for EC-Number 1.3.1.100)
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Release 2023.1 (January 2023)
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