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Literature summary for 1.4.3.26 extracted from

  • 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 (2019), J. Am. Chem. Soc., 141, 13582-13591 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.3.26

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mycobacterium ulcerans
expression in Escherichia coli Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 Mycobacterium ulcerans
-
 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
 ?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 Mycolicibacterium smegmatis
-
 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
 ?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 Mycobacterium ulcerans Agy99
-
 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
 ?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 Mycolicibacterium smegmatis ATCC 700084
-
 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 Mycobacterium ulcerans
-
 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 Mycolicibacterium smegmatis
-
 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 Mycobacterium ulcerans Agy99
-
 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 Mycolicibacterium smegmatis ATCC 700084
-
 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
-
 ?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O Mycobacterium ulcerans
-
 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
 ?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O Mycolicibacterium smegmatis
-
 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
 ?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O Mycobacterium ulcerans Agy99
-
 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
 ?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O Mycolicibacterium smegmatis ATCC 700084
-
 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
 ?
additional information Mycobacterium ulcerans 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 Mycolicibacterium smegmatis 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 Mycobacterium ulcerans Agy99 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 Mycolicibacterium smegmatis ATCC 700084 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 ?
-
-

Organism

Organism UniProt Comment Textmining
Mycobacterium ulcerans A0PM50
-
-
Mycobacterium ulcerans Agy99 A0PM50
-
-
Mycolicibacterium smegmatis A0QSB9
-
-
Mycolicibacterium smegmatis ATCC 700084 A0QSB9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
-
 Mycobacterium ulcerans 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
 ?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
-
 Mycolicibacterium smegmatis 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
 ?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
-
 Mycobacterium ulcerans Agy99 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
-
 ?
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2
-
 Mycolicibacterium smegmatis ATCC 700084 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
-
 Mycobacterium ulcerans 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
-
 Mycolicibacterium smegmatis 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
-
 Mycobacterium ulcerans Agy99 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
-
 Mycolicibacterium smegmatis ATCC 700084 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2
-
 ?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
-
 Mycobacterium ulcerans 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
 ?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
-
 Mycolicibacterium smegmatis 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
 ?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
-
 Mycobacterium ulcerans Agy99 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3
-
 ?
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O
-
 Mycolicibacterium smegmatis ATCC 700084 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 Mycobacterium ulcerans ?
-
-
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 Mycolicibacterium smegmatis ?
-
-
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 Mycolicibacterium smegmatis ?
-
-
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 Mycobacterium ulcerans ?
-
-
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 Mycobacterium ulcerans Agy99 ?
-
-
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 Mycobacterium ulcerans Agy99 ?
-
-
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 Mycolicibacterium smegmatis ATCC 700084 ?
-
-
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 Mycolicibacterium smegmatis ATCC 700084 ?
-
-

Synonyms

Synonyms Comment Organism
IldD1
-
 Mycobacterium ulcerans
mftD
-
 Mycobacterium ulcerans
mftD
-
 Mycolicibacterium smegmatis
msmeg 1424
-
 Mycolicibacterium smegmatis
mul_0774
-
 Mycobacterium ulcerans

Cofactor

Cofactor Comment Organism Structure
FMN
-
 Mycobacterium ulcerans
FMN
-
 Mycolicibacterium smegmatis

General Information

General Information Comment Organism
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 Mycolicibacterium smegmatis