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Literature summary extracted from

  • Aly, K.A.; Beebe, E.T.; Chan, C.H.; Goren, M.A.; Sepulveda, C.; Makino, S.; Fox, B.G.; Forest, K.T.
    Cell-free production of integral membrane aspartic acid proteases reveals zinc-dependent methyltransferase activity of the Pseudomonas aeruginosa prepilin peptidase PilD (2013), MicrobiologyOpen, 2, 94-104.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.4.23.43 synthesis scaled-up synthesis of PilD, followed by solubilization in dodecyl-beta-D-maltoside and chromatography, leads to a pure enzyme that retains its known biochemical activities Pseudomonas aeruginosa
3.4.23.52 synthesis scaled-up synthesis of PilD, followed by solubilization in dodecyl-beta-D-maltoside and chromatography, leads to a pure enzyme that retains its known biochemical activities Methanococcus voltae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.23.43 Zn2+ PilD is a zinc-binding protein. Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage Pseudomonas aeruginosa
3.4.23.52 Zn2+ PilD is a zinc-binding protein. Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage Methanococcus voltae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.43 additional information Pseudomonas aeruginosa enzyme additionally catalyzes S-adenosyl methionine-dependent methylation of the mature pilin ?
-
 ?
3.4.23.43 additional information Pseudomonas aeruginosa ATCC 15692 enzyme additionally catalyzes S-adenosyl methionine-dependent methylation of the mature pilin ?
-
 ?
3.4.23.43 prepilin PilA + H2O Pseudomonas aeruginosa
-
 ? cosynthesis of PilD with its full-length substrate, PilA, leads to complete cleavage of the substrate signal peptides ?
3.4.23.43 prepilin PilA + H2O Pseudomonas aeruginosa ATCC 15692
-
 ? cosynthesis of PilD with its full-length substrate, PilA, leads to complete cleavage of the substrate signal peptides ?
3.4.23.52 FlaB2 + H2O Methanococcus voltae
-
 ? cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.43 Pseudomonas aeruginosa P22610
-
-
3.4.23.43 Pseudomonas aeruginosa ATCC 15692 P22610
-
-
3.4.23.52 Methanococcus voltae Q8NKW5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.43 additional information enzyme additionally catalyzes S-adenosyl methionine-dependent methylation of the mature pilin Pseudomonas aeruginosa ?
-
 ?
3.4.23.43 additional information enzyme additionally catalyzes S-adenosyl methionine-dependent methylation of the mature pilin Pseudomonas aeruginosa ATCC 15692 ?
-
 ?
3.4.23.43 prepilin PilA + H2O
-
 Pseudomonas aeruginosa ? cosynthesis of PilD with its full-length substrate, PilA, leads to complete cleavage of the substrate signal peptides ?
3.4.23.43 prepilin PilA + H2O
-
 Pseudomonas aeruginosa ATCC 15692 ? cosynthesis of PilD with its full-length substrate, PilA, leads to complete cleavage of the substrate signal peptides ?
3.4.23.52 FlaB2 + H2O
-
 Methanococcus voltae ? cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides ?

Synonyms

EC Number Synonyms Comment Organism
3.4.23.43 PilD
-
 Pseudomonas aeruginosa
3.4.23.52 FlaK
-
 Methanococcus voltae