Information on EC 2.4.1.337 - 1,2-diacylglycerol 3-alpha-glucosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.337
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RECOMMENDED NAME
GeneOntology No.
1,2-diacylglycerol 3-alpha-glucosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
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UDP-glucose + 1,2-diacyl-sn-glycerol = UDP + 3-D-glucosyl-1,2-diacyl-sn-glycerol
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alpha-diglucosyldiacylglycerol biosynthesis
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Glycerolipid metabolism
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Metabolic pathways
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type IV lipoteichoic acid biosynthesis (S. pneumoniae)
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SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:1,2-diacyl-sn-glycerol 3-alpha-D-glucosyltransferase
The enzyme from the bacterium Acholeplasma laidlawii, which lacks a cell wall, produces the major non-bilayer lipid in the organism. The enzyme from the bacterium Agrobacterium tumefaciens acts under phosphate deprivation, generating glycolipids as surrogates for phospholipids. The enzyme belongs to the GT4 family of configuration-retaining glycosyltransferases. Many diacylglycerols with long-chain acyl groups can act as acceptors. cf. EC 2.4.1.336, monoglucosyldiacylglycerol synthase.
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
UDP-alpha-D-glucose + 1,2-dioleoyl-sn-glycerol
UDP + 1,2-dioleoyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
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-
-
-
?
UDP-alpha-D-glucose + 1,2-dipalmitoyl-sn-glycerol
UDP + 1,2-dipalmitoyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
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-
-
-
?
UDP-alpha-D-glucose + a 1,2-diacyl-sn-glycerol
UDP + a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
UDP-alpha-D-glucuronic acid + a 1,2-diacyl-sn-glycerol
UDP + a 1,2-diacyl-3-O-(alpha-D-glucuronosyl)-sn-glycerol
show the reaction diagram
UDP-glucose + 1,2-dioleoylglycerol
UDP + 3-D-glucosyl-1,2-dioleoylglycerol
show the reaction diagram
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?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
UDPglucose + 1,2-dipalmitoylglycerol
UDP + 3-D-glucosyl-1,2-dipalmitoylglycerol
show the reaction diagram
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twice as high enzyme activity as sn-1,2-dioleoylglycerol at all concentrations up to 2.5 mol% concentration
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?
additional information
?
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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
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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strong dependence on, maximal activity at 15-28 mM MgCl2
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-dioleoyl-sn-glycero-3-phosphoglycerol
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activates
CHAPS
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In CHAPS detergent, mixed micelles, enzyme shows a cooperative dependence on anionic lipids for activity
dioleoyl-phosphatidylglycerol
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stimulates the enzyme by an activating, potentially cooperative mechanism. Physiological concentrations of dioleoyl-phosphatidylglycerol influence the turnover number of the enzyme but not the interaction with UDP-glucose
dodecylphosphoglycerol
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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; can stimulate the MGlcDAG synthase activity efficiently with a concomitant protection toward proteolytic digestion
phosphatidylglycerol
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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
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activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37 - 0.44
UDP-alpha-D-glucose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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1 * 40000, SDS-PAGE; x * 40000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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1 * 40000, SDS-PAGE; x * 40000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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half-life is around 50 h
20
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half-life is around 1.8 h
28
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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
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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C or -50C, stable for at least 48 days
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-20C, stable for at least 48 days
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20C, 100 mM KH2PO4/K2HPO4, pH 8, 20% (v/v) glycerol, and 20 mM CHAPS, half-life 1.8 h
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4C, 100 mM KH2PO4/K2HPO4, pH 8, 20% (v/v) glycerol, and 20 mM CHAPS, half-life 50h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Binding of the enzyme to lipid bilayers containing biological fractions of anionic lipids is essentially irreversible under most conditions examined. Binding is strongly influenced by anionic lipids, by nonbilayer-prone molecules and by charged polypeptides. Binding to membranes follows a two-step process. The binding is faster and stronger by electrostatic attraction, but hydrophobic interactions are also involved in enhancing the binding and activation process. Once the enzyme is bound to the membrane, it is practically glued in an irreversible fashion
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during purification, the concentration of detergent is just as important as the type of detergent, and a low concentration of n-dodecyl-beta-D-maltoside (about 1 x critical micelle concentration) is the best for keeping the protein stable and homogeneous
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proteolytic resistance shows a good correlation with the enzyme activity in various lipid-CHAPS mixed micelles. Anionic lipids 1,2-dioleoyl-phosphatidylglycerol and 1,2-dioleoyl-posphatidylserine are able to protect the exposed MGlc-DAG synthase from digestion, whereas 1,2-dioleoyl-phosphatidylcholine and diglucosyldiacylglycerol can not. The detergent dodecylphosphoglycerol can also stimulate the MGlcDAG synthase activity efficiently with a concomitant protection toward proteolytic digestion
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
critical fractions of anionic phospholipids 1,2-dioleoyl-phosphatidylglycerol and 1,2-dioleoyl-posphatidylserine are essential for the restoration of enzyme activity, while the zwitterionic 1,2-dioleoyl-phosphatidylcholine and the uncharged diglucosyldiacylglycerol are not
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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optimization of protein expression through controlling a few basic expression parameters, including temperature and growth media. The final expression level can be increased by two orders of magnitude, reaching 170 mg of pure protein per litre culture