| 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] |
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| [EC 3.4.14.14 created 2021] |
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