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Literature summary for 3.6.1.62 extracted from

  • Floor, S.; Borja, M.; Gross, J.
    Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan (2012), Proc. Natl. Acad. Sci. USA, 109, 2872-2877.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.62

Cloned(Commentary)

Cloned (Comment) Organism
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 Saccharomyces cerevisiae
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 Schizosaccharomyces pombe

Protein Variants

Protein Variants Comment Organism
W43A mutation at Trp43 blocks kinetic stimulation by subunit Dcp1 Schizosaccharomyces pombe
W50A Mutation in subunit Dcp2. While the wild-type Dcp1-Dcp2 complex is stimulated by enhancer of decapping Edc1CTR by a factor of 13, it only enhances catalysis in the W50A mutant by a factor of three. Coactivation of decapping by Dcp2 is linked to formation of the composite active site Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P53550
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Schizosaccharomyces pombe O13828
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Schizosaccharomyces pombe ATCC 24843 O13828
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information residue Trp43 of subunit Dcp2 is a conserved gatekeeper of the open-to-closed transition that controls the decapping reaction. Dcp2 samples multiple conformations in solution on the millisecond-microsecond timescale. Mutation of the gatekeeper tryptophan abolishes the dynamic behavior of Dcp2 and attenuates coactivation by yeast enhancer of decapping Edc1. Subunit Dcp1 directly contacts the catalytic domain of subunit Dcp2. Coactivation of decapping by Dcp2 is linked to formation of the composite active site Schizosaccharomyces pombe ?
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 ?
additional information residue Trp43 of subunit Dcp2 is a conserved gatekeeper of the open-to-closed transition that controls the decapping reaction. Dcp2 samples multiple conformations in solution on the millisecond-microsecond timescale. Mutation of the gatekeeper tryptophan abolishes the dynamic behavior of Dcp2 and attenuates coactivation by yeast enhancer of decapping Edc1. Subunit Dcp1 directly contacts the catalytic domain of subunit Dcp2. Coactivation of decapping by Dcp2 is linked to formation of the composite active site Schizosaccharomyces pombe ATCC 24843 ?
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 ?

Subunits

Subunits Comment Organism
More subunit Dcp1 directly contacts the catalytic domain of subunit Dcp2. Coactivation of decapping by Dcp2 is linked to formation of the composite active site Schizosaccharomyces pombe