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Information on EC 2.1.1.293 - 6-hydroxytryprostatin B O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.293
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.293 6-hydroxytryprostatin B O-methyltransferase
IUBMB Comments
Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, fumitremorgins and verruculogen.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
ftmD, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ftmD
ftmD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 6-hydroxytryprostatin B = S-adenosyl-L-homocysteine + tryprostatin A
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
fumitremorgin C biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine + 6-hydroxytryprostatin B = S-adenosyl-L-homocysteine + tryprostatin A
Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, fumitremorgins and verruculogen.
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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
S-adenosyl-L-methionine + 6-hydroxytryprostatin B
S-adenosyl-L-homocysteine + tryprostatin A
S-adenosyl-L-methionine + 6-hydroxytryprostatin B
S-adenosyl-L-homocysteine + tryprostatin A
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-hydroxytryprostatin B
S-adenosyl-L-homocysteine + tryprostatin A
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-hydroxytryprostatin B
S-adenosyl-L-homocysteine + tryprostatin A
Substrates: -
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
S-adenosyl-L-methionine + 6-hydroxytryprostatin B
S-adenosyl-L-homocysteine + tryprostatin A
S-adenosyl-L-methionine + 6-hydroxytryprostatin B
S-adenosyl-L-homocysteine + tryprostatin A
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-hydroxytryprostatin B
S-adenosyl-L-homocysteine + tryprostatin A
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 6-hydroxytryprostatin B
S-adenosyl-L-homocysteine + tryprostatin A
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
0.021
6-hydroxytryprostatin B
wild type enzyme, at pH 6.8 and 15°C
0.12
6-hydroxytryprostatin B
mutant enzyme R202L, at pH 6.8 and 15°C
0.0045
S-adenosyl-L-methionine
mutant enzyme R202L, at pH 6.8 and 15°C
0.011
S-adenosyl-L-methionine
wild type enzyme, at pH 6.8 and 15°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.2
6-hydroxytryprostatin B
mutant enzyme R202L, at pH 6.8 and 15°C
2 - 8
S-adenosyl-L-methionine
wild type enzyme, at pH 6.8 and 15°C
6.9
S-adenosyl-L-methionine
mutant enzyme R202L, at pH 6.8 and 15°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
66
6-hydroxytryprostatin B
mutant enzyme R202L, at pH 6.8 and 15°C
1300
6-hydroxytryprostatin B
wild type enzyme, at pH 6.8 and 15°C
1500
S-adenosyl-L-methionine
mutant enzyme R202L, at pH 6.8 and 15°C
2500
S-adenosyl-L-methionine
wild type enzyme, at pH 6.8 and 15°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
the wild type enzyme shows about 42% activity at pH 6.0, about 78% activity at pH 6.5, and about 90% activity at pH 7.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
the wild type enzyme shows 100% activity at 10°C, about 95% activity at 20°C, about 75% activity at 30°C, about 35% activity at 35°C, and no activity at 40°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Af293 R202L variant; isolates Af293, A1163 and BM939, gene ftmD
UniProt
brenda
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
evolution
all ftm genes are expressed almost equally well in both Af293 and BM939 strains. But a point mutation found in ftmD in the genome of Af293 causes an arginine to leucine substitution at position 202 of FtmD, resulting in a dramatic decrease of the catalytic efficiency of FtmD. This mutated form of FtmD appeared not functioning under physiological conditions in Af293 to produce any detectable levels of TPS-A or any downstream metabolites
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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). FTMD_NEOFI
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181)
411
0
45863
Swiss-Prot
-
FTMD_ASPFU
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)
342
0
38436
Swiss-Prot
-
A0A8H4GSY9_9EURO
411
0
46035
TrEMBL
Secretory Pathway (Reliability: 1)
B0YAZ3_ASPFC
Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10)
411
0
45569
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R202L
additional information
engineered production of tryprostatins in Escherichia coli through reconstitution of a partial ftm biosynthetic gene cluster from Aspergillus sp., i.e. four genes, ftmABCD, on two compatible plasmids
R202L
the mutant has 19.7times lower catalytic efficiency compared to the wild type enzyme
R202L
-
the mutant has 19.7times lower catalytic efficiency compared to the wild type enzyme
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ftmD, encoded in the ftm gene cluster, recombinant expression in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kato, N.; Suzuki, H.; Okumura, H.; Takahashi, S.; Osada, H.
A point mutation in ftmD blocks the fumitremorgin biosynthetic pathway in Aspergillus fumigatus strain Af293
Biosci. Biotechnol. Biochem.
77
1061-1067
2013
Aspergillus fumigatus (B9WZX2), Aspergillus fumigatus Af293 (B9WZX2)
brenda
Shah, G.R.; Wesener, S.R.; Cheng, Y.Q.
Engineered production of tryprostatins in E. coli through reconstitution of a partial ftm biosynthetic gene cluster from Aspergillus sp.
Jacobs J. Biotechnol. Bioeng.
2
009
2015
Aspergillus fumigatus (Q4WAW6)
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.293)
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Release 2026.1 (March 2026)
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