26 lines
1.1 KiB
Markdown
26 lines
1.1 KiB
Markdown
---
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title: "AdoMet MTase"
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chunk: 1/1
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source: "https://en.wikipedia.org/wiki/AdoMet_MTase"
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category: "reference"
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tags: "science, encyclopedia"
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date_saved: "2026-05-05T11:26:05.398611+00:00"
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instance: "kb-cron"
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---
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S-adenosylmethionine-dependent methyltransferase (SAM-MTase or AdoMet-MTase) is a conserved protein domain and protein superfamily. SAM-MTase proteins are methyltransferases. There are five protein families within SAM-MTase,
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SAM-MTases use S-adenosyl-L-methionine as a substrate for methylation, creating the product S-adenosyl-L-homocysteine.
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== Structure and subgroups ==
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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.
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A review published in 2003 divides all methyltransferases into 5 main classes based on the structure of their catalytic domain (fold):
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class I: Rossmann-like α/β, the largest subgroup.
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class II: TIM β/α-barrel α/β
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class III: tetrapyrrole methylase α/β
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class IV: SPOUT α/β
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class V: SET domain all β
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== References == |