AdoMet MTase
| SAM-dependent MTases superfamily | |
|---|---|
| Identifiers | |
| Symbol | SAM-dependent_MTases |
| InterPro | IPR029063 |
| AdoMet_MTase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | AdoMet_MTase | ||||||||
| Pfam | PF07757 | ||||||||
| Pfam clan | CL0063 | ||||||||
| InterPro | IPR011671 | ||||||||
| |||||||||
S-adenosylmethionine-dependent methyltransferase (SAM-MTase or AdoMet-MTase) is a conserved protein domain and protein superfamily.[1] SAM-MTase proteins are methyltransferases.[2] There are five protein families within SAM-MTase,
SAM-MTases use S-adenosyl-L-methionine as a substrate for methylation, creating the product S-adenosyl-L-homocysteine.[3]
Structure and subgroups[edit]
All SAM-MTases contain a structurally conserved SAM-binding domain consisting of a central seven-stranded beta-sheet that is flanked by three alpha-helices per side of the sheet.[4]
A review published in 2003 divides all methyltransferases into 5 main classes based on the structure of their catalytic domain (fold):[5]
- class I: Rossmann-like α/β, the largest subgroup.[3]
- class II: TIM β/α-barrel α/β
- class III: tetrapyrrole methylase α/β
- class IV: SPOUT α/β
- class V: SET domain all β
References[edit]
- ^ Wang, Jiyao; Chitsaz, Farideh; Derbyshire, Myra K.; Gonzales, Noreen R.; Gwadz, Marc; Lu, Shennan; Marchler, Gabriele H.; Song, James S.; Thanki, Narmada; Yamashita, Roxanne A.; Yang, Mingzhang; Zhang, Dachuan; Zheng, Chanjuan; Lanczycki, Christopher J.; Marchler-Bauer, Aron (2023-01-06). "The conserved domain database in 2023". Nucleic Acids Research. 51 (D1): D384–D388. doi:10.1093/nar/gkac1096. ISSN 1362-4962. PMC 9825596. PMID 36477806.
- ^ Knizewski L, Ginalski K (July 2006). "DUF1613 is a novel family of eucaryotic AdoMet-dependent methyltransferases". Cell Cycle. 5 (14): 1580–2. doi:10.4161/cc.5.14.2978. PMID 16861910.
- ^ a b "CDD Conserved Protein Domain Family: AdoMet_MTases". www.ncbi.nlm.nih.gov. Retrieved 2023-12-07.
- ^ Martin, Jennifer L; McMillan, Fiona M (2002-12-01). "SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold". Current opinion in structural biology. 12 (6): 783–793. doi:10.1016/s0959-440x(02)00391-3. ISSN 1879-033X. PMID 12504684.
- ^ Schubert, Heidi L; Blumenthal, Robert M; Cheng, Xiaodong (2003-06-01). "Many paths to methyltransfer: a chronicle of convergence". Trends in biochemical sciences. 28 (6): 329–335. doi:10.1016/s0968-0004(03)00090-2. ISSN 0968-0004. PMC 2758044. PMID 12826405.
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