EC 4.4.1.36 - Hercynylcysteine S-oxide lyase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 4.4.1.36

Names

Accepted name:
hercynylcysteine S-oxide lyase
Other name:
egtE (gene name)
Systematic name:
S-(hercyn-2-yl)-L-cysteine ergothioneine-sulfenate-lyase

Reaction

Cofactor

Comments:

Contains pyridoxal 5'-phosphate. The enzyme, characterized from the bacterium Mycobacterium smegmatis, cayalyses the last step in the pathway of ergothioneine biosynthesis. The enzyme forms a 2-sulfenohercynine intermediate, which is reduced to ergothioneine non-enzymically by a thiol. In vitro, DTT can serve this function.

The enzyme, characterized from the bacterium Mycobacterium smegmatis, cayalyses the last step in the pathway of ergothioneine biosynthesis. The enzyme forms a 2-sulfenohercynine intermediate, which is reduced to ergothioneine non-enzymically by a thiol. In vitro, DTT can serve this function.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB

References

  1. Seebeck, F. P.
    In vitro reconstitution of Mycobacterial ergothioneine biosynthesis.
    J. Am. Chem. Soc. 132: 6632-6633 (2010). [PMID: 20420449]
  2. Pluskal, T., Ueno, M., Yanagida, M.
    Genetic and metabolomic dissection of the ergothioneine and selenoneine biosynthetic pathway in the fission yeast, S. pombe, and construction of an overproduction system.
    PLoS ONE 9: e97774 (2014). [PMID: 24828577]
  3. Song, H., Hu, W., Naowarojna, N., Her, A. S., Wang, S., Desai, R., Qin, L., Chen, X., Liu, P.
    Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediate.
    Sci Rep 5: 11870 (2015). [PMID: 26149121]

[EC 4.4.1.36 created 2017]