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x * 25000, isoform Plsp1, SDS-PAGE
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x * 29000, isoform Plsp2, SDS-PAGE
dimer
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1 * 52000 + 1 * 55000, SDS-PAGE
dimer
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1 * 50000 (beta-MPP) + 1 * 53000 (alpha-MPP), recombinant enzyme, SDS-PAGE
dimer
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1 * 48000 (MAS1) + 1 * 51000 (MAS2), Saccharomyces cerevisiae, SDS-PAGE
dimer
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1 * 48800 (MAS1) + 1 * 51800 (MAS2), Saccharomyces cerevisiae, calculated from amino acid sequence
dimer
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MPP is a heterodimeric enzyme consisting of regulatory alpha-MPP and catalytic beta-MPP subunits, analysis of the fluorescence resonance energy transfer between EGFP fused to a yeast aconitase presequence and regiospecific 7-dietylamino-3-(4'-maleimidyl phenyl)-4-methyl coumarin-labelled yeast MPPs, plausible model of preEGFP associated with MPP constructed in silico, structure modeling, overview
dimer
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1 * 48000 (MAS1) + 1 * 51000 (MAS2), Saccharomyces cerevisiae, SDS-PAGE
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heterodimer
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heterodimer
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alphaMPP and betaMPP
heterodimer
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consists of a alpha-mitochondrial processing peptidase and beta-MPP
heterodimer
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alpha and beta subunit of HPP, both subunits required to function most efficiently. Yeast alpha subunit of MPP does not interact with the Trichomonas beta subunit of HPP. Trichomonas alpha subunit of HPP is able to form a heterodimer with yeast beta subunit of MPP
monomer
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beta subunit, functions efficiently as a single subunit monomer, data indicate that the monomeric enzyme evolved from an ancestral heterodimeric MPP comprising both an alpha and a beta subunit
monomer
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1 * 57000, Neurospora crassa, MPP protein, SDS-PAGE
monomer
1 * 45578, alphabeta, sequence calculation
monomer
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1 * 45578, alphabeta, sequence calculation
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additional information
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processing activity is optimal at a 1:1 molar ratio of alpha- and beta-MPP
additional information
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subunits do not form a stable complex
additional information
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The mitochondrial processing peptidase from Neurospora crassa consists of two components: MPP and processing enhancing protein
additional information
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MPP alone has a low processing activity, processing enhancing protein alone has none, upon recombining both, full processing activity is restored, both proteins cooperate in binding precursor substrates and proteolytic activity, the latter is associated with the MPP protein (MW 57000)
additional information
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alpha-MPP (formerly MAS2) alone has no catalytic activity
additional information
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MAS2 activity alone is very low, MAS1 restores activity
additional information
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Saccharomyces cerevisiae has two loosely associated non-identical subunits that dissociate upon gel filtration
additional information
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homology between MAS1 and MAS2 amino acid sequences
additional information
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the large subunit alone has no cleavage activity
additional information
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Saccharomyces cerevisiae has two loosely associated non-identical subunits that dissociate upon gel filtration
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additional information
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the large subunit alone has no cleavage activity
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additional information
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sequence homologies between P55, P53 from potato and processing enhancing protein from yeast or Neurospora crassa and between P51 from potato and MPP from yeast or Neurospora crassa
additional information
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the mitochondrial processing peptidase components of cytochrome c reductase-processing peptidase complex are the three largest subunits: P55, P53 and P51, with MW 55000, 53000 and 51000, respectively, SDS-PAGE
additional information
TTHA1264 possesses two repetitive domains with a canonical fold for peptidase family M16. The betaMPP subunit contains the zinc-binding motif essential for peptidase activity, while subunit alphaMPP instead possesses a glycine-rich loop, which is proposed to be important for substrate recognition or restriction. Structure analysis, modelling, overview
additional information
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TTHA1264 possesses two repetitive domains with a canonical fold for peptidase family M16. The betaMPP subunit contains the zinc-binding motif essential for peptidase activity, while subunit alphaMPP instead possesses a glycine-rich loop, which is proposed to be important for substrate recognition or restriction. Structure analysis, modelling, overview
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