Information on EC 2.1.1.110 - sterigmatocystin 8-O-methyltransferase

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The expected taxonomic range for this enzyme is: Aspergillus

EC NUMBER
COMMENTARY hide
2.1.1.110
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RECOMMENDED NAME
GeneOntology No.
sterigmatocystin 8-O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + dihydrosterigmatocystin = S-adenosyl-L-homocysteine + 8-O-methyldihydrosterigmatocystin
show the reaction diagram
(2)
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-
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S-adenosyl-L-methionine + sterigmatocystin = S-adenosyl-L-homocysteine + 8-O-methylsterigmatocystin
show the reaction diagram
(1)
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-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aflatoxin biosynthesis
-
-
aflatoxins B1 and G1 biosynthesis
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aflatoxins B2 and G2 biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:sterigmatocystin 8-O-methyltransferase
Dihydrosterigmatocystin can also act as acceptor. Involved in the biosynthesis of aflatoxins in fungi.
CAS REGISTRY NUMBER
COMMENTARY hide
116958-29-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 3357
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + dihydrosterigmatocystin
S-adenosyl-L-homocysteine + dihydro-8-O-methylsterigmatocystin
show the reaction diagram
S-adenosyl-L-methionine + sterigmatocystin
S-adenosyl-L-homocysteine + 8-O-methylsterigmatocystin
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + sterigmatocystin
S-adenosyl-L-homocysteine + 8-O-methylsterigmatocystin
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
-
0.1 mM, 58% inhibition
Fe2+
-
0.1 mM, 87% inhibition
Hg2+
-
0.1 mM, complete inhibition
Phenylmercuriacetate
-
0.1 mM, 96% inhibition
S-adenosyl-L-homocysteine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0096 - 0.042
S-adenosyl-L-methionine
0.0018 - 0.002
sterigmatocystin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022 - 2.2
sterigmatocystin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012
S-adenosyl-L-homocysteine
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 60
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approx. 35% of maximal activity at 25°C, approx. 30% of maximal activity at 60°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
x * 40000, SRRC 163, SDS-PAGE, the 40000 Da protein is distinct from the 168000 Da methyl transferase purified from the same fungal strain
58000
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1 * 110000 + 1 * 58000, SRCC 163, SDS-PAGE
110000
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1 * 110000 + 1 * 58000, SRCC 163, SDS-PAGE
160000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
strain SRRC 163, anion exchange, hydroxylapatite, DEAE-Sperodex, octyl avidgel, anion-exchange
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strain SRRC 2043, ultracentrifugation, ammonium sulfate, DEAE-Sephadex, immunoaffinity column
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