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Details on Person CDK5RAP1, a homolog of bacterial miaB, is a SAM radical enzy...
| Class:Id | Summation:9936982 |
|---|---|
| _displayName | CDK5RAP1, a homolog of bacterial miaB, is a SAM radical enzy... |
| _timestamp | 2025-02-05 14:27:24 |
| created | [InstanceEdit:9936995] May, Bruce, 2025-01-28 |
| literatureReference | [LiteratureReference:9936971] Adenosylmethionine as a source of 5'-deoxyadenosyl radicals [LiteratureReference:9936969] Structural basis for tRNA methylthiolation by the radical SAM enzyme MiaB [LiteratureReference:9936932] Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases |
| modified | [InstanceEdit:9937665] May, Bruce, 2025-02-05 |
| text | CDK5RAP1, a homolog of bacterial miaB, is a SAM radical enzyme that uses a 5-deoxyadenosine radical to remove a hydrogen atom from the C2 atom of adenosine (Fontecave et al. 2001, Forouhar et al. 2013, Esakova et al. 2021). A methyl group and a sulfur atom are then added to form a 2-methylthio group. The source of the methyl group may be S-adenosylmethionine. The source of the sulfur is unknown. The initial substrate is tRNA(Ser)(UCN) (MT-TS1) that contains the modification N6-dimethylallyladenosine-37.and the product is 2-methylthio-N6-dimethylallyladenosine-37 MT-TS1 (Reiter et al. 2012, also inferred from mouse homolog). |
| (summation) | [BlackBoxEvent:9937017] CDK5RAP1 thiomethylates dimethylallyladenosine-37 of mitochondrial tRNA(Ser)(UCN) (MT-TS1) [Homo sapiens] |
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