Information on EC 2.4.1.157 - 1,2-diacylglycerol 3-glucosyltransferase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
2.4.1.157
-
RECOMMENDED NAME
GeneOntology No.
1,2-diacylglycerol 3-glucosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-glucose + 1,2-diacyl-sn-glycerol = UDP + 3-D-glucosyl-1,2-diacyl-sn-glycerol
show the reaction diagram
-
-
-
-
UDP-glucose + 1,2-diacyl-sn-glycerol = UDP + 3-D-glucosyl-1,2-diacyl-sn-glycerol
show the reaction diagram
electrostatic association of the enzyme with membrane surface is accompanied by hydrophobic interactions and a conformational change. Binding kinetics fit a two-state model
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glycerolipid metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:1,2-diacyl-sn-glycerol 3-D-glucosyltransferase
Many diacylglycerols with long-chain acyl groups can act as acceptors.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glucosyltransferase, uridine diphosphoglucose-diacylglycerol
-
-
-
-
MGlcDG synthase
-
-
monoglucosyldiacylglycerol synthase
-
-
UDP-glucose-diacylglycerol glucosyltransferase
-
-
-
-
UDP-glucose:1,2-diacylglycerol glucosyltransferase
-
-
-
-
UDPglucose:1,2-diacylglycerol 3-D-glucosyltransferase
-
-
-
-
UDPglucose:diacylglycerol glucosyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
83744-96-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Marburg strain 60015
-
-
Manually annotated by BRENDA team
putative 1,2-diacylglycerol 3-glucosyltransferase, fragment; strain ACA-DC 198
Uniprot
Manually annotated by BRENDA team
putative 1,2-diacylglycerol 3-glucosyltransferase, fragment; strain ACA-DC 198
Uniprot
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + 1,2-dioleoylglycerol
UDP + 3-D-glucosyl-1,2-dioleoylglycerol
show the reaction diagram
-
-
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
-
-
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
-
-
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
-
-
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
-
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
-
the enzyme successively transfers up to four glucose residues to 1,2-diacylglycerol. The starting activity can be characterized as a UDP-glucose:1,2-diacylglycerol-3-beta-D-glucosyltransferase, whereas in subsequent steps the glucose acceptors vary and represent the products of previous additions of beta-glucosyl residues
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
-
the enzyme synthesizes the major nonbilayer-prone lipid monoglucosyldiacylglycerol in the membrane, which is important for spontaneous curvature, and is an important site for the lipid surface charge density
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
-
the enzyme synthesizes the major nonbilayer-prone lipid monoglucosyldiacylglycerol in the membrane, which is important for spontaneous curvature, and is an important site for the lipid surface charge density
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
-
the product monoglucosyldiacylglycerol is the first glucolipid along the glucolipid pathway, and a major nonbilayer-prone lipid in the single membrane
-
-
?
UDPglucose + 1,2-dipalmitoylglycerol
UDP + 3-D-glucosyl-1,2-dipalmitoylglycerol
show the reaction diagram
-
-
-
-
?
UDPglucose + 1,2-dipalmitoylglycerol
UDP + 3-D-glucosyl-1,2-dipalmitoylglycerol
show the reaction diagram
-
-
-
-
?
UDPglucose + 1,2-dipalmitoylglycerol
UDP + 3-D-glucosyl-1,2-dipalmitoylglycerol
show the reaction diagram
-
twice as high enzyme activity as sn-1,2-dioleoylglycerol at all concentrations up to 2.5 mol% concentration
-
-
?
UDPglucose + 1-oleoyl-2-palmitoylglycerol
UDP + 3-D-glucosyl-1-oleoyl-2-palmitoylglycerol
show the reaction diagram
-
-
-
-
?
UDPglucose + 1-stearoyl-2-palmitoylglycerol
UDP + 3-D-glucosyl-1-stearoyl-2-palmitoylglycerol
show the reaction diagram
-
-
-
-
?
additional information
?
-
B0JFC0, -
enzyme is induced upon at least some of the acid-adapting conditions, involved in the biosynthesis of the glycolipid moiety that anchors lipoteichoic acid onto the bacterial cell membrane
-
-
-
additional information
?
-
B0JFC0
enzyme is induced upon at least some of the acid-adapting conditions, involved in the biosynthesis of the glycolipid moiety that anchors lipoteichoic acid onto the bacterial cell membrane
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
-
the enzyme synthesizes the major nonbilayer-prone lipid monoglucosyldiacylglycerol in the membrane, which is important for spontaneous curvature, and is an important site for the lipid surface charge density
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
-
the enzyme synthesizes the major nonbilayer-prone lipid monoglucosyldiacylglycerol in the membrane, which is important for spontaneous curvature, and is an important site for the lipid surface charge density
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
-
the product monoglucosyldiacylglycerol is the first glucolipid along the glucolipid pathway, and a major nonbilayer-prone lipid in the single membrane
-
-
?
additional information
?
-
B0JFC0, -
enzyme is induced upon at least some of the acid-adapting conditions, involved in the biosynthesis of the glycolipid moiety that anchors lipoteichoic acid onto the bacterial cell membrane
-
-
-
additional information
?
-
B0JFC0
enzyme is induced upon at least some of the acid-adapting conditions, involved in the biosynthesis of the glycolipid moiety that anchors lipoteichoic acid onto the bacterial cell membrane
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
required, maximal activity at 20 mM MgCl2
Mg2+
-
strong dependence on, maximal activity at 15-28 mM MgCl2
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,2-dioleoyl-sn-glycero-3-phosphoglycerol
-
activates
phosphatidylglycerol
-
anionic amphiphiles are essential for the restoration of a proper conformation. Amphiphilic environment with a critical fraction of negatively charged headgroups induces a catalytic, active site conformation of the enzyme
sn-1,2-dioleoylglycerol
-
activates
dodecylphosphoglycerol
-
anionic amphiphiles are essential for the restoration of a proper conformation. Amphiphilic environment with a critical fraction of negatively charged headgroups induces a catalytic, active site conformation of the enzyme
additional information
-
the activity measured at 30C does not differ between control and heat-shocked cells. However, activity assayed at 42C is higher than that assayed at 30C for both the non-heat-shocked and heat-shocked cells, indicating that MGlcDG synthase activity is largely affected by reaction temperature but not by heat shock during growth, activity assayed at 42C for heat-shocked cells is slightly higher than that for non-heat-shocked cells
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.045
-
UDPglucose
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8.7
-
pH 5.0: about 45% of maximal activity, pH 8.7: about 50% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28
55
-
28C: 50% of maximal activity, 55C: 35% of maximal activity
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
plasma membranes, thylakoid membranes, not in outer membrane
Manually annotated by BRENDA team
-
associated with, in vitro enzyme binds less efficiently to liposomes containing only zwitterionic lipids whereas increasing fractions of anionic phosphatidyglycerol or cardiolipin strongly promote binding
Manually annotated by BRENDA team
additional information
-
almost no activity is observed in the soluble fraction
-
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
1 * 40000, SDS-PAGE
?
-
x * 44000, SDS-PAGE
?
-
x * 43600, SDS-PAGE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
half-life is around 50 h
20
-
-
half-life is around 1.8 h
28
-
-
half-life in 1,2-dioleoylphosphatidylglycerol-CHAPS micelles is more than 2 h, half-life is less than 0.5 h in 1,2-dioleoylphosphatidylcholine-CHAPS micelles
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
total digestion by proteinase K, trypsin or chymotrypsin when no lipid is present, the activity is highly restored in micelles containing 1,2-dioleoyl-phosphatidylglycerol and 1,2-dioleoyl-phosphatidylserine
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C or -50C, stable for at least 48 days
-
-80C, stable for at least 2 months, crude enzyme extract
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ni-NTA column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
temperature-dependent activation of Sll1377 expression is observed in the membrane fraction of Synechocystis sp. PCC 6803, whereas the Sll1377 protein level remains unchanged, suggesting that the activity is posttranslationally regulated without covalent modification of Sll1377 by soluble enzymes
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D147Q
-
the mutant has almost no activity and blocks temperature-dependent activation, suggesting that these amino acid residue is essential for Sll1377 activity at both normal growth temperature and the higher temperature
D200A
-
the mutant has almost no activity and blocks temperature-dependent activation, suggesting that these amino acid residue is essential for Sll1377 activity at both normal growth temperature and the higher temperature
R329Q
-
the mutant significantly reduces the activity and blocks temperature-dependent activation, suggesting that these amino acid residue is essential for Sll1377 activity at both normal growth temperature and the higher temperature
R331A
-
the mutant has almost no activity and blocks temperature-dependent activation, suggesting that these amino acid residue is essential for Sll1377 activity at both normal growth temperature and the higher temperature