Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline S-adenosyl-L-methionine Identifier CHEBI:59789 Charge 1 Formula C15H23N6O5S InChIKeyhelp_outline MEFKEPWMEQBLKI-AIRLBKTGSA-O SMILEShelp_outline C[S+](CC[C@H]([NH3+])C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 842 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-homoserine lactone Identifier CHEBI:58633 Charge 1 Formula C4H8NO2 InChIKeyhelp_outline QJPWUUJVYOJNMH-VKHMYHEASA-O SMILEShelp_outline [NH3+][C@H]1CCOC1=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-methyl-5'-thioadenosine Identifier CHEBI:17509 (Beilstein: 42420; CAS: 2457-80-9) help_outline Charge 0 Formula C11H15N5O3S InChIKeyhelp_outline WUUGFSXJNOTRMR-IOSLPCCCSA-N SMILEShelp_outline CSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 33 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:21932 | RHEA:21933 | RHEA:21934 | RHEA:21935 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Enzymatic cleavage of S-adenosylmethionine.
MUDD S.H.
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The mechanism of the enzymatic cleavage of S-adenosylmethionine to alpha-amino-gamma-butyrolactone.
MUDD S.H.
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Structure and mechanism of a phage-encoded SAM lyase revises catalytic function of enzyme family.
Guo X., Soederholm A., Kanchugal P.S., Isaksen G.V., Warsi O., Eckhard U., Trigueis S., Gogoll A., Jerlstroem-Hultqvist J., Aaqvist J., Andersson D.I., Selmer M.
The first S-adenosyl methionine (SAM) degrading enzyme (SAMase) was discovered in bacteriophage T3, as a counter-defense against the bacterial restriction-modification system, and annotated as a SAM hydrolase forming 5'-methyl-thioadenosine (MTA) and L-homoserine. From environmental phages, we rec ... >> More
The first S-adenosyl methionine (SAM) degrading enzyme (SAMase) was discovered in bacteriophage T3, as a counter-defense against the bacterial restriction-modification system, and annotated as a SAM hydrolase forming 5'-methyl-thioadenosine (MTA) and L-homoserine. From environmental phages, we recently discovered three SAMases with barely detectable sequence similarity to T3 SAMase and without homology to proteins of known structure. Here, we present the very first phage SAMase structures, in complex with a substrate analogue and the product MTA. The structure shows a trimer of alpha-beta sandwiches similar to the GlnB-like superfamily, with active sites formed at the trimer interfaces. Quantum-mechanical calculations, thin-layer chromatography, and nuclear magnetic resonance spectroscopy demonstrate that this family of enzymes are not hydrolases but lyases forming MTA and L-homoserine lactone in a unimolecular reaction mechanism. Sequence analysis and in vitro and in vivo mutagenesis support that T3 SAMase belongs to the same structural family and utilizes the same reaction mechanism. << Less