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Literature summary for 3.4.21.105 extracted from

  • Maegawa, S.; Koide, K.; Ito, K.; Akiyama, Y.
    The intramembrane active site of GlpG, an E. coli rhomboid protease, is accessible to water and hydrolyses an extramembrane peptide bond of substrates (2007), Mol. Microbiol., 64, 435-447.
    View publication on PubMed
Search for more literature for 3.4.21.105

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the intramembrane enzyme possesses a intramembraneously located active site, which is accessible to water and hydrolyses an extramembrane peptide bond of substrates Escherichia coli 16020
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Organism

Organism UniProt Comment Textmining
Escherichia coli P09391 gene glpG
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Bla-GknTM-MBP + H2O recombinantly expressed fusion protein having the transmembrane region of Gurken, GknTM, a physiological substrate of Drosophila rhomboids, GlpG cleaves an extramembrane region of the substrate exposed to the periplasm, overview Escherichia coli ?
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additional information the intramembrane enzyme possesses a intramembraneously located active site, which is accessible to water and hydrolyses an extramembrane peptide bond of substrates, membrane-embedded polypeptide segments of substrates enter at lateral entrance into the enzyme’s active site Escherichia coli ?
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protein Bla-LY2-MBP + H2O recombinantly expressed type I model membrane protein substrate having the second transmembrane region of lactose permease LY2 at the extramembrane region in vivo and in vitro at the predicted periplasm-membrane boundary region of LY2, the determinants for proteolysis reside within the LY2 sequence, GlpG cleaves an extramembrane region of the substrate exposed to the periplasm, overview Escherichia coli ?
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Synonyms

Synonyms Comment Organism
GlpG
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 Escherichia coli