Methionine gamma-lyase
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FunctionMethionine γ-lyase (MGL) degrades sulfur-containing amino acids to α-keto acids, ammonia and thiols. It catalyzes the interconversion of L-methionine and water to methanethiol, ammonia and 2-oxobutanoate. MGL uses pyridoxal phosphate (PLP) as cofactor[1]. Structural highlightsMGL active site contains the cofactor PLP[2]. 3D Structures of methionine γ-lyaseMethionine gamma-lyase 3D structures
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ReferencesReferences
- ↑ Goyer A, Collakova E, Shachar-Hill Y, Hanson AD. Functional characterization of a methionine gamma-lyase in Arabidopsis and its implication in an alternative to the reverse trans-sulfuration pathway. Plant Cell Physiol. 2007 Feb;48(2):232-42. Epub 2006 Dec 13. PMID:17169919 doi:http://dx.doi.org/10.1093/pcp/pcl055
- ↑ Mamaeva DV, Morozova EA, Nikulin AD, Revtovich SV, Nikonov SV, Garber MB, Demidkina TV. Structure of Citrobacter freundii L-methionine gamma-lyase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jun 1;61(Pt, 6):546-9. Epub 2005 Jun 1. PMID:16511092 doi:10.1107/S1744309105015447