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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 4.4.1.11

Accepted Name
Methionine gamma-lyase.
Alternative Name(s)
L-methioninase.
Methionine lyase.
Reaction catalysed
L-methionine + H(2)O <=> methanethiol + NH(3) + 2-oxobutanoate
Cofactor(s)
Pyridoxal 5'-phosphate.
Comment(s)
  • The enzyme cleaves a carbon-sulfur bond, releasing methanethiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia.
  • The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10.
  • The enzyme is involved in L-methionine catabolism.
Cross-references
PROSITEPDOC00677
BRENDA4.4.1.11
EC2PDB4.4.1.11
ExplorEnz4.4.1.11
PRIAM enzyme-specific profiles4.4.1.11
KEGG Ligand Database for Enzyme Nomenclature4.4.1.11
IUBMB Enzyme Nomenclature4.4.1.11
IntEnz4.4.1.11
MEDLINEFind literature relating to 4.4.1.11
MetaCyc4.4.1.11
UniProtKB/Swiss-Prot
Q8RDT4, MEGL_FUSNN;  Q8L0X4, MEGL_FUSNP;  Q7MX71, MEGL_PORGI;  
A0A0J6G7P5, MEGL_PSEDM;  P13254, MEGL_PSEPU;  Q826W3, MEGL_STRAW;  
Q73KL7, MEGL_TREDE;  Q9SGU9, MGL_ARATH;  

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.4.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-