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Enzyme Nomenclature
Information on EC 1.4.3.26 - pre-mycofactocin synthase
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1.4.3.26 pre-mycofactocin synthaseIUBMB Comments
A flavoprotein (FMN). The enzyme participates in the biosynthesis of the enzyme cofactor mycofactocin. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an alpha-keto moiety on the resulting molecule.
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The expected taxonomic range for this enzyme is: Mycobacteriaceae
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IldD1
mftD
msmeg 1424
mul_0774
mftD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O = 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
(overall reaction)
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-
-
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 = 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
(1a)
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5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O = 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
(1b), spontaneous
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SYSTEMATIC NAME
IUBMB Comments
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one:oxygen oxidoreductase
A flavoprotein (FMN). The enzyme participates in the biosynthesis of the enzyme cofactor mycofactocin. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an alpha-keto moiety on the resulting molecule.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
-
-
-
?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
-
-
?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
-
-
?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
-
-
?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
-
-
?
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety
-
-
-
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule
-
-
-
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety
-
-
-
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule
-
-
-
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety
-
-
-
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone , forming an 2-oxo moiety on the resulting premycofactocin molecule
-
-
-
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety
-
-
-
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone , forming an 2-oxo moiety on the resulting premycofactocin molecule
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
-
-
-
?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
-
-
-
?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
-
-
?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
-
-
?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
-
-
?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
-
-
?
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety
-
-
-
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety
-
-
-
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety
-
-
-
additional information
?
-
MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
disruption of any of the genes of the Mft cluster results in impaired growth of Mycobacterium marinum in cholesterol:EtOH. Functionality of Mft is strictly required for growth of free-living mycobacteria in ethanol and other primary alcohols
physiological function
disruption of any of the genes of the Mft cluster results in impaired growth of Mycobacterium tuberculosis in cholesterol:EtOH. Functionality of Mft is strictly required for growth of free-living mycobacteria in ethanol and other primary alcohols
physiological function
disruption of any of the genes of the Mft cluster results in impaired growth of Mycolicibacterium smegmatis in cholesterol:EtOH. Functionality of Mft is strictly required for growth of free-living mycobacteria in ethanol and other primary alcohols
physiological function
premycofactocin is a biologically active redox cofactor that oxidizes NADH bound by Mycobycterium smegmatis carveol dehydrogenase and can be used by carveol dehydrogenase in the oxidation of carveol
physiological function
-
premycofactocin is a biologically active redox cofactor that oxidizes NADH bound by Mycobycterium smegmatis carveol dehydrogenase and can be used by carveol dehydrogenase in the oxidation of carveol
-
physiological function
-
disruption of any of the genes of the Mft cluster results in impaired growth of Mycolicibacterium smegmatis in cholesterol:EtOH. Functionality of Mft is strictly required for growth of free-living mycobacteria in ethanol and other primary alcohols
-
physiological function
-
disruption of any of the genes of the Mft cluster results in impaired growth of Mycobacterium tuberculosis in cholesterol:EtOH. Functionality of Mft is strictly required for growth of free-living mycobacteria in ethanol and other primary alcohols
-
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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). MFTD_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
399
0
42774
Swiss-Prot
-
MFTD_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
396
0
42161
Swiss-Prot
-
MFTD_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
396
0
42161
Swiss-Prot
-
MFTD_MYCUA
Mycobacterium ulcerans (strain Agy99)
390
0
41780
Swiss-Prot
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ayikpoe, R.; Latham, J.
MftD catalyzes the formation of a biologically active redox center in the biosynthesis of the ribosomally synthesized and post-translationally modified redox cofactor mycofactocin
J. Am. Chem. Soc.
141
13582-13591
2019
Mycobacterium ulcerans (A0PM50), Mycolicibacterium smegmatis (A0QSB9), Mycobacterium ulcerans Agy99 (A0PM50), Mycolicibacterium smegmatis ATCC 700084 (A0QSB9)
brenda
Krishnamoorthy, G.; Kaiser, P.; Lozza, L.; Hahnke, K.; Mollenkopf, H.; Kaufmann, S.
Mycofactocin is associated with ethanol metabolism in mycobacteria
mBio
10
e00190
2019
Mycobacterium marinum, Mycolicibacterium smegmatis (A0QSB9), Mycobacterium tuberculosis (P9WND7), Mycolicibacterium smegmatis ATCC 700084 (A0QSB9), Mycobacterium tuberculosis H37Rv (P9WND7)
brenda
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Release 2023.1 (January 2023)
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