Information on EC 2.5.1.42 - geranylgeranylglycerol-phosphate geranylgeranyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.5.1.42
-
RECOMMENDED NAME
GeneOntology No.
geranylgeranylglycerol-phosphate geranylgeranyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
geranylgeranyl diphosphate + 3-(O-geranylgeranyl)-sn-glycerol 1-phosphate = diphosphate + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkenyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
CDP-archaeol biosynthesis
-
-
lipid metabolism
-
-
Glycerophospholipid metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
geranylgeranyl diphosphate:sn-3-O-(geranylgeranyl)glycerol 1-phosphate geranylgeranyltransferase
This enzyme is an integral-membrane protein that carries out the second prenyltransfer reaction involved in the formation of polar membrane lipids in Archaea. Requires a divalent metal cation, such as Mg2+ or Mn2+, for activity [2]. 4-Hydroxybenzoate, 1,4-dihydroxy 2-naphthoate, homogentisate and alpha-glycerophosphate cannot act as prenyl-acceptor substrates [2]. The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 1.1.1.261 (sn-glycerol-1-phosphate dehydrogenase), EC 2.5.1.41 (phosphoglycerol geranylgeranyltransferase), which, together with this enzyme, alkylates the hydroxy groups of glycerol 1-phosphate to yield unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 (CDP-archaeol synthase) to form CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [3]. Belongs in the UbiA prenyltransferase family [2].
CAS REGISTRY NUMBER
COMMENTARY hide
124650-68-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
geranylgeranyl diphosphate + (S)-3-O-(geranylgeranyl)glycerol 1-phosphate
diphosphate + 2,3-bis-O-(geranylgeranyl)glycerol 1-phosphate
show the reaction diagram
geranylgeranyl diphosphate + 3-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
geranylgeranyl diphosphate + 3-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
show the reaction diagram
Q9UWY6
the enzyme carries out the second prenyltransfer reaction involved in the formation of polar membrane lipids in archaea
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
divalent metal ion required, optimal activity with 10 mM Mg2+. 40% of maximal activity is obtrained with 10 mM Ca2+. 1 mM Ca2+ hardly activates
Mg2+
requirement of a divalent metal ion for activity. 1 mM Mg2+ gives 40% of the activity with 10 mM Mg2+
Mn2+
divalent metal ion required, optimal activity with 10 mM Mg2+. 10 mM Mn2+ leads to severely decreased activity
Zn2+
divalent metal ion required, optimal activity with 10 mM Mg2+. 10 mM Zn2+ leads to severely decreased activity. 1 mM Zn2+ hardly activates
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 28000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli with a hexameric histidine tag
Show AA Sequence (340 entries)
Please use the Sequence Search for a certain query.