Literature summary for 3.4.23.52 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.

Search for more literature for 3.4.23.52

Application

Application	Comment	Organism
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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
FlaB2 + H2O	Methanococcus voltae	-	?	cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides	?

Organism

Organism	UniProt	Comment	Textmining
Methanococcus voltae	Q8NKW5	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
FlaB2 + H2O	-	Methanococcus voltae	?	cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides	?

Synonyms

Synonyms	Comment	Organism
FlaK	-	Methanococcus voltae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)