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ENZYME

ENZYME entry: EC 4.4.1.42

Accepted Name
S-adenosyl-L-methionine lyase
Alternative Name(s)
adenosylmethionine cyclotransferase
S-adenosyl-L-methionine alkyltransferase (cyclizing)
SAM lyase
Reaction catalysed
S-adenosyl-L-methionine <=> L-homoserine lactone + S-methyl-5'-thioadenosine
Comment(s)
  • The enzyme was originally described from the yeast Saccharomyces cerevisiae (as EC 2.5.1.4), though it had not been well characterized.
  • It was also incorrectly described from several bacteriophages as a hydrolase (EC 3.13.2.2).
  • Later work has shown the bacteriophage enzyme to be a lyase.
  • The enzyme binds its substrate at the border between two subunits of a trimeric complex in a position that prevents it from interacting with water.
  • Instead, the substrate reacts with itself and splits in two. The product, L-homoserine lactone, spontaneously hydrolyzes to L-homoserine.
  • Formerly EC 2.5.1.4 and EC 3.13.2.2.
Cross-references
BRENDA4.4.1.42
EC2PDB4.4.1.42
ExplorEnz4.4.1.42
PRIAM enzyme-specific profiles4.4.1.42
KEGG Ligand Database for Enzyme Nomenclature4.4.1.42
IUBMB Enzyme Nomenclature4.4.1.42
IntEnz4.4.1.42
MEDLINEFind literature relating to 4.4.1.42
MetaCyc4.4.1.42
Rhea expert-curated reactions4.4.1.42
UniProtKB/Swiss-Prot
P07693, ADOM_BPT3

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