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Literature summary for 3.4.21.107 extracted from

  • Ge, X.; Wang, R.; Ma, J.; Liu, Y.; Ezemaduka, A.N.; Chen, P.R.; Fu, X.; Chang, Z.
    DegP primarily functions as a protease for the biogenesis of beta-barrel outer membrane proteins in the Gram-negative bacterium Escherichia coli (2014), FEBS J., 281, 1226-1240.
    View publication on PubMed
Search for more literature for 3.4.21.107

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FkpA + H2O Escherichia coli periplasmic peptidyl-prolyl cis–trans isomerase, chaperone ?
-
 ?
MalE + H2O Escherichia coli periplasmic maltose-binding protein ?
-
 ?
additional information Escherichia coli identification of beta-barrel outer membrane proteins, OMPs, as major natural substrates by photo-crosslinking using non-natural amino acid DiZPK, 3-(3-methyl-3H-diazirine-3-yl)-propaminocarbonyl-Nepsilon-L-lysine, as the photo-crosslinker. Isoform DegP primarily functions as a protease, at both low and high temperatures, to eliminate unfolded outer membrane proteins, with hardly any appreciable chaperone activity in cells. The toxic and cell membrane-damaging misfolded outer membrane proteins would accumulate in DegP-lacking cells cultured under heat shock conditions ?
-
 ?
OmpA + H2O Escherichia coli outer membrane porin protein ?
-
 ?
OmpC + H2O Escherichia coli outer membrane porin protein ?
-
 ?
OmpF + H2O Escherichia coli outer membrane porin protein ?
-
 ?
OmpW + H2O Escherichia coli outer membrane porin protein ?
-
 ?
OmpX + H2O Escherichia coli outer membrane porin protein ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FkpA + H2O periplasmic peptidyl-prolyl cis–trans isomerase, chaperone Escherichia coli ?
-
 ?
FkpA + H2O periplasmic peptidyl-prolyl cis-trans isomerase, chaperone Escherichia coli ?
-
 ?
MalE + H2O periplasmic maltose-binding protein Escherichia coli ?
-
 ?
additional information identification of beta-barrel outer membrane proteins, OMPs, as major natural substrates by photo-crosslinking using non-natural amino acid DiZPK, 3-(3-methyl-3H-diazirine-3-yl)-propaminocarbonyl-Nepsilon-L-lysine, as the photo-crosslinker. Isoform DegP primarily functions as a protease, at both low and high temperatures, to eliminate unfolded outer membrane proteins, with hardly any appreciable chaperone activity in cells. The toxic and cell membrane-damaging misfolded outer membrane proteins would accumulate in DegP-lacking cells cultured under heat shock conditions Escherichia coli ?
-
 ?
OmpA + H2O outer membrane porin protein Escherichia coli ?
-
 ?
OmpC + H2O outer membrane porin protein Escherichia coli ?
-
 ?
OmpF + H2O outer membrane porin protein Escherichia coli ?
-
 ?
OmpW + H2O outer membrane porin protein Escherichia coli ?
-
 ?
OmpX + H2O outer membrane porin protein Escherichia coli ?
-
 ?