S-Adenosylmethionine synthetase enzyme
| Methionine adenosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
ExPASy NiceZyme view | | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
S-Adenosylmethionine synthetase (
Function
AdoMet is a
As a
SAM is also involved in
This article discusses the protein domains that make up the SAM synthetase enzyme and how these domains contribute to its function. More specifically, this article explores the shared pseudo-3-fold symmetry that makes the domains well-adapted to their functions.[6]
This enzyme catalyses the following chemical reaction
- ATP + L-methionine + H2O S-adenosyl-L-methionine
Conserved motifs in the 3'UTR of MAT2A mRNA
A computational comparative analysis of vertebrate
Protein overview
The S-adenosylmethionine synthetase enzyme is found in almost every organism bar parasites which obtain AdoMet from their host.
S-adenosylmethionine synthetase N terminal domain
| S-adenosylmethionine synthetase N terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| |||||||||
In
N terminal domain function
The N terminal domain is well conserved across different species. This may be due to its important function in
N terminal domain structure
The N terminal region contains two alpha helices and four beta strands.[6]
S-adenosylmethionine synthetase Central domain
| S-adenosylmethionine synthetase Central domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| |||||||||
Central terminal domain function
The precise function of the central domain has not been fully elucidated, but it is thought to be important in aiding catalysis.
Central domain Structure
The central region contains two alpha helices and four beta strands.[6]
S-adenosylmethionine synthetase, C terminal domain
| S-adenosylmethionine synthetase, C-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| |||||||||
In
C terminal domain function
The function of the C-terminal domain has been experimentally determined as being important for cytoplasmic localisation. The residues are scattered along the C-terminal domain sequence however once the protein folds, they position themselves closely together.[3]
C terminal domain Structure
The C-terminal domains contains two alpha-helices and four beta-strands.[6]
References
External links
- Methionine+adenosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EC 2.5.1.6
