The Enzyme Database

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EC 1.3.98.7     
Accepted name: [mycofactocin precursor peptide]-tyrosine decarboxylase
Reaction: C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine = C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5′-deoxyadenosine + L-methionine
Other name(s): mftC (gene name)
Systematic name: C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine L-tyrosine-carboxylyase
Comments: This is a bifunctional radical AdoMet (radical SAM) enzyme that catalyses the first two steps in the biosynthesis of the enzyme cofactor mycofactocin. Activity requires the presence of the MftB chaperone. The other activity of the enzyme is EC 4.1.99.26, 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Haft, D.H. Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners. BMC Genomics 12:21 (2011). [DOI] [PMID: 21223593]
2.  Bruender, N.A. and Bandarian, V. The radical S-adenosyl-L-methionine enzyme MftC catalyzes an oxidative decarboxylation of the C-terminus of the MftA peptide. Biochemistry 55 (2016) 2813–2816. [DOI] [PMID: 27158836]
3.  Khaliullin, B., Ayikpoe, R., Tuttle, M. and Latham, J.A. Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC. J. Biol. Chem. 292 (2017) 13022–13033. [DOI] [PMID: 28634235]
4.  Ayikpoe, R., Ngendahimana, T., Langton, M., Bonitatibus, S., Walker, L.M., Eaton, S.S., Eaton, G.R., Pandelia, M.E., Elliott, S.J. and Latham, J.A. Spectroscopic and electrochemical characterization of the mycofactocin biosynthetic protein, MftC, provides insight into its redox flipping mechanism. Biochemistry 58 (2019) 940–950. [DOI] [PMID: 30628436]
[EC 1.3.98.7 created 2021]
 
 
EC 1.4.3.26     
Accepted name: pre-mycofactocin synthase
Reaction: 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)
(1a) 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 = 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2
(1b) 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O = 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 (spontaneous)
Glossary: 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione = pre-mycofactocinone = PMFT
Other name(s): mftD (gene name)
Systematic name: 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one:oxygen oxidoreductase
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 α-keto moiety on the resulting molecule.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ayikpoe, R.S. and Latham, J.A. 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 (2019) 13582–13591. [DOI] [PMID: 31381312]
[EC 1.4.3.26 created 2020]
 
 
EC 3.4.14.14     
Accepted name: [mycofactocin precursor peptide] peptidase
Reaction: C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + H2O = C-terminal [mycofactocin precursor peptide]-glycine + 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one
Glossary: 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one = AHDP
Other name(s): mftE (gene name)
Systematic name: C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one hydrolyase
Comments: Requires Fe2+ ad Zn2+. The enzyme participates in the biosynthesis of the enzyme cofactor mycofactocin. It catalyses cleavage of the mycofactocin precursor peptide following its modification by MftC to liberate its final two residues, which consist of a cross-linked valine-tyramine dipeptide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bruender, N.A. and Bandarian, V. The creatininase homolog MftE from Mycobacterium smegmatis catalyzes a peptide cleavage reaction in the biosynthesis of a novel ribosomally synthesized post-translationally modified peptide (RiPP). J. Biol. Chem. 292 (2017) 4371–4381. [DOI] [PMID: 28077628]
2.  Ayikpoe, R., Salazar, J., Majestic, B. and Latham, J.A. Mycofactocin biosynthesis proceeds through 3-amino-5-[(p-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone (AHDP); direct observation of MftE specificity toward MftA. Biochemistry 57 (2018) 5379–5383. [DOI] [PMID: 30183269]
[EC 3.4.14.14 created 2021]
 
 
EC 4.1.99.26     
Accepted name: 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthase
Reaction: C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5′-deoxyadenosine + L-methionine + A = C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2
Other name(s): mftC (gene name)
Systematic name: C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one lyase (C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol-forming)
Comments: This is a bifunctional radical AdoMet (radical SAM) enzyme that catalyses the first two steps in the biosynthesis of the enzyme cofactor mycofactocin. Activity requires the presence of the MftB chaperone. The reaction occurs in the right-to-left direction. The other activity of the enzyme is EC 1.3.98.7, [mycofactocin precursor peptide]-tyrosine decarboxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Haft, D.H. Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners. BMC Genomics 12:21 (2011). [DOI] [PMID: 21223593]
2.  Bruender, N.A. and Bandarian, V. The radical S-adenosyl-L-methionine enzyme MftC catalyzes an oxidative decarboxylation of the C-terminus of the MftA peptide. Biochemistry 55 (2016) 2813–2816. [DOI] [PMID: 27158836]
3.  Khaliullin, B., Ayikpoe, R., Tuttle, M. and Latham, J.A. Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC. J. Biol. Chem. 292 (2017) 13022–13033. [DOI] [PMID: 28634235]
4.  Ayikpoe, R., Ngendahimana, T., Langton, M., Bonitatibus, S., Walker, L.M., Eaton, S.S., Eaton, G.R., Pandelia, M.E., Elliott, S.J. and Latham, J.A. Spectroscopic and electrochemical characterization of the mycofactocin biosynthetic protein, MftC, provides insight into its redox flipping mechanism. Biochemistry 58 (2019) 940–950. [DOI] [PMID: 30628436]
[EC 4.1.99.26 created 2021]
 
 


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