Structural highlights
Function
A0A0A5P8W7_CITFR
Publication Abstract from PubMed
Interactions of Citrobacter freundii methionine gamma-lyase (MGL) with sulfoxides of typical substrates were investigated. It was found that sulfoxides are suicide substrates of the enzyme. The products of the beta- and gamma-elimination reactions of sulfoxides, thiosulfinates, oxidize three cysteine residues of the enzyme. Three-dimensional structures of MGL inactivated by dimethyl thiosulfinate and diethyl thiosulfinate were determined at 1.46A and 1.59A resolution. Analysis of the structures identified SH groups oxidized by thiosulfinates and revealed the structural bases of MGL inactivation. The extent of inactivation of MGL in the catalysis of the beta-elimination reaction depends on the length of the <<tail>> at oxidized Cys115. Oxidation of Cys115 results in MGL incapable to catalyze the stage of methyl mercaptan elimination of the physiological reaction.
Sulfoxides of sulfur-containing amino acids are suicide substrates of Citrobacter freundii methionine gamma-lyase. Structural bases of the enzyme inactivation.,Revtovich S, Morozova E, Kulikova V, Koval V, Anufrieva N, Nikulin A, Demidkina T Biochimie. 2020 Jan;168:190-197. doi: 10.1016/j.biochi.2019.11.004. Epub 2019 Nov, 9. PMID:31711941[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Revtovich S, Morozova E, Kulikova V, Koval V, Anufrieva N, Nikulin A, Demidkina T. Sulfoxides of sulfur-containing amino acids are suicide substrates of Citrobacter freundii methionine gamma-lyase. Structural bases of the enzyme inactivation. Biochimie. 2020 Jan;168:190-197. doi: 10.1016/j.biochi.2019.11.004. Epub 2019 Nov, 9. PMID:31711941 doi:http://dx.doi.org/10.1016/j.biochi.2019.11.004
