Literature summary for 3.1.3.27 extracted from

Kumaran, D.; Bonanno, J.B.; Burley, S.K.; Swaminathan, S.
Crystal structure of phosphatidylglycerophosphatase (PGPase), a putative membrane-bound lipid phosphatase, reveals a novel binuclear metal binding site and two "proton wires" (2006), Proteins, 64, 851-862.

Search for more literature for 3.1.3.27

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21 (DE3) cells	Listeria monocytogenes

Crystallization (Commentary)

Crystallization (Comment)	Organism
with precipitant containing 30% pentaerythritol ethoxylate, 50 mM ammonium sulfate, 50 mM Bis-Tris at pH 6.5	Listeria monocytogenes

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	each protomer contains an independent active site with two metal ions, Ca2+ and Mg2+, forming a heterobinuclear center located in a hydrophilic cavity near the surface of the molecule	Listeria monocytogenes
Mg2+	each protomer contains an independent active site with two metal ions, Ca2+ and Mg2+, forming a heterobinuclear center located in a hydrophilic cavity near the surface of the molecule	Listeria monocytogenes

Organism

Organism	UniProt	Comment	Textmining
Listeria monocytogenes	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
phosphatidylglycerol 3-phosphate + H2O	-	Listeria monocytogenes	phosphatidylglycerol + phosphate	-	?

Subunits

Subunits	Comment	Organism
homotetramer	x-ray crystallography	Listeria monocytogenes

Synonyms

Synonyms	Comment	Organism
PGPase	-	Listeria monocytogenes

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)