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Information on EC 2.4.1.337 - 1,2-diacylglycerol 3-alpha-glucosyltransferase
for references in articles please use BRENDA:EC2.4.1.337
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.337 1,2-diacylglycerol 3-alpha-glucosyltransferase
IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
- 2.4.1.337
- acholeplasma
-
bilayer
- laidlawii
-
curvature
-
nonbilayer-prone
-
nonbilayer
- phosphatidylglycerol
- phospholipids
- liposome
- phosphatidylethanolamine
- lactose
-
zwitterionic
-
permease
-
liquid-crystalline
- synthesis
Reaction Schemes
showSynonyms
mglcdag synthase, atu2297, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Atu2297
EC 2.4.1.157
-
-
formerly, part transferred
-
MGS
UDP-glucose-diacylglycerol glucosyltransferase
-
-
-
-
UDP-glucose:1,2-diacyl-sn-glycerol 3-D-glucosyltransferase
-
-
-
-
UDP-glucose:1,2-diacylglycerol 3-D-glucosyltransferase
-
-
-
-
UDP-glucose:1,2-diacylglycerol glucosyltransferase
-
-
-
-
UDP-glucose:diacylglycerol glucosyltransferase
-
-
-
-
UgtP
uridine diphosphoglucose-diacylglycerol glucosyltransferase
-
-
-
-
MGS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
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
-
-
-
-
UDP-glucose + 1,2-diacyl-sn-glycerol = UDP + 3-D-glucosyl-1,2-diacyl-sn-glycerol
electrostatic association of the enzyme with membrane surface is accompanied by hydrophobic interactions and a conformational change. Binding kinetics fit a two-state model
UDP-glucose + 1,2-diacyl-sn-glycerol = UDP + 3-D-glucosyl-1,2-diacyl-sn-glycerol
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
alpha-diglucosyldiacylglycerol biosynthesis, 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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
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
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + 1,2-dipalmitoyl-sn-glycerol
UDP + 1,2-dipalmitoyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + a 1,2-diacyl-sn-glycerol
UDP + a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
UDP-alpha-D-glucuronic acid + a 1,2-diacyl-sn-glycerol
UDP + a 1,2-diacyl-3-O-(alpha-D-glucuronosyl)-sn-glycerol
UDP-glucose + 1,2-dioleoylglycerol
UDP + 3-D-glucosyl-1,2-dioleoylglycerol
Substrates: -
Products: -
Products: -
?
UDPglucose + 1,2-dipalmitoylglycerol
UDP + 3-D-glucosyl-1,2-dipalmitoylglycerol
Substrates: twice as high enzyme activity as sn-1,2-dioleoylglycerol at all concentrations up to 2.5 mol% concentration
Products: -
Products: -
?
UDP-alpha-D-glucose + a 1,2-diacyl-sn-glycerol
UDP + a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + a 1,2-diacyl-sn-glycerol
UDP + a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
Agrobacterium tumefaciens ATCC 33970
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucuronic acid + a 1,2-diacyl-sn-glycerol
UDP + a 1,2-diacyl-3-O-(alpha-D-glucuronosyl)-sn-glycerol
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucuronic acid + a 1,2-diacyl-sn-glycerol
UDP + a 1,2-diacyl-3-O-(alpha-D-glucuronosyl)-sn-glycerol
Agrobacterium tumefaciens ATCC 33970
Substrates: -
Products: -
Products: -
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
Substrates: -
Products: -
Products: -
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
Substrates: -
Products: -
Products: -
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
Substrates: 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
Products: -
Products: -
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
-
Substrates: 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
Products: -
Products: -
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
Substrates: the product monoglucosyldiacylglycerol is the first glucolipid along the glucolipid pathway, and a major nonbilayer-prone lipid in the single membrane
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzymic activity depends on the bilayer lipid environment. The activity depends on membrane binding per se but the enzyme must also adopt a certain conformation or orientation, and activity can be substantially modulated by interaction with various charged lipids or soluble molecules
Products: -
Products: -
?
additional information
?
-
Substrates: enzymic activity depends on the bilayer lipid environment. The activity depends on membrane binding per se but the enzyme must also adopt a certain conformation or orientation, and activity can be substantially modulated by interaction with various charged lipids or soluble molecules
Products: -
Products: -
?
additional information
?
-
Substrates: promiscuous glycosyltransferase, usues UDP-glucose or UDP-glucuronic acid as sugar donors
Products: -
Products: -
?
additional information
?
-
-
Substrates: promiscuous glycosyltransferase, usues UDP-glucose or UDP-glucuronic acid as sugar donors
Products: -
Products: -
?
additional information
?
-
Agrobacterium tumefaciens ATCC 33970
Substrates: promiscuous glycosyltransferase, usues UDP-glucose or UDP-glucuronic acid as sugar donors
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
Substrates: 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
Products: -
Products: -
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
-
Substrates: 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
Products: -
Products: -
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
Substrates: the product monoglucosyldiacylglycerol is the first glucolipid along the glucolipid pathway, and a major nonbilayer-prone lipid in the single membrane
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CHAPS
In CHAPS detergent, mixed micelles, enzyme shows a cooperative dependence on anionic lipids for activity
dioleoyl-phosphatidylglycerol
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
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
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
dodecylphosphoglycerol
can stimulate the MGlcDAG synthase activity efficiently with a concomitant protection toward proteolytic digestion
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.37
UDP-alpha-D-glucose
pH 8.0, 28°C, presence of 31 mol% CHAPS
0.39
UDP-alpha-D-glucose
pH 8.0, 28°C, presence of 20 mol% CHAPS
0.44
UDP-alpha-D-glucose
pH 8.0, 28°C, presence of 25 mol% CHAPS
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
enzyme deletion mutants lacking monoglucosyl diacylglycerol and glucuronosyl diacylglycerol or all glycolipids are not impaired in growth or virulence during infection of tobacco leaf discs
physiological function
the abnormal morphology of a UgtP mutant is caused by lack of glucolipids. Expression of a monoglucosyldiacylglycerol produced by 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii (alMGS) almost completely suppresses the UgtP disruptant phenotype. Activation of extracytoplasmic function sigmas (SigM, SigV, and SigX) in the UgtP mutant is decreased by alMGS expression, and is suppressed to low levels by MgSO4 addition. When alMGS and Acholeplasma laidlawii 1,2-diacylglycerol-3-glucose (1->2)-glucosyltransferase producing diglucosyldiacylglycerol are simultaneously expressed, SigX activation is repressed to wild type level
physiological function
the abnormal morphology of a UgtP mutant is caused by lack of glucolipids. Expression of a monoglucosyldiacylglycerol produced by 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii (alMGS) almost completely suppresses the UgtP disruptant phenotype. Activation of extracytoplasmic function sigmas (SigM, SigV, and SigX) in the UgtP mutant is decreased by alMGS expression, and is suppressed to low levels by MgSO4 addition. When alMGS and Acholeplasma laidlawii 1,2-diacylglycerol-3-glucose (1->2)-glucosyltransferase producing diglucosyldiacylglycerol are simultaneously expressed, SigX activation is repressed to wild type level
physiological function
-
the abnormal morphology of a UgtP mutant is caused by lack of glucolipids. Expression of a monoglucosyldiacylglycerol produced by 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii (alMGS) almost completely suppresses the UgtP disruptant phenotype. Activation of extracytoplasmic function sigmas (SigM, SigV, and SigX) in the UgtP mutant is decreased by alMGS expression, and is suppressed to low levels by MgSO4 addition. When alMGS and Acholeplasma laidlawii 1,2-diacylglycerol-3-glucose (1->2)-glucosyltransferase producing diglucosyldiacylglycerol are simultaneously expressed, SigX activation is repressed to wild type level
-
physiological function
Agrobacterium tumefaciens ATCC 33970
-
enzyme deletion mutants lacking monoglucosyl diacylglycerol and glucuronosyl diacylglycerol or all glycolipids are not impaired in growth or virulence during infection of tobacco leaf discs
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AMGDS_STRR6
441
0
50306
Swiss-Prot
-
PADGT_ACHLA
332
0
38447
Swiss-Prot
other Location (Reliability: 2)
Q7CXE5_AGRFC
Agrobacterium fabrum (strain C58 / ATCC 33970)
349
0
38691
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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
20°C, 100 mM KH2PO4/K2HPO4, pH 8, 20% (v/v) glycerol, and 20 mM CHAPS, half-life 1.8 h
4°C, 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
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
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
LITERATURE
synthesis
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, L.; Karlsson, O.P.; Wieslander, A.
Activating amphiphiles cause a conformational change of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes according to proteolytic digestion
J. Biol. Chem.
272
29602-29606
1997
Acholeplasma laidlawii, Acholeplasma laidlawii (Q93P60)
brenda
Berg, S.; Edman, M.; Li, L.; Wikstrom, M.; Wieslander, A.
Sequence properties of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes: recognition of a large group of lipid glycosyltransferases in eubacteria and archaea
J. Biol. Chem.
276
22056-22063
2001
Acholeplasma laidlawii
brenda
Karlsson, O.P.; Dahlqvist, A.; Vikstroem, S.; Wieslander, A.
Lipid dependence and basic kinetics of the purified 1,2-diacylglycerol 3-glucosyltransferase from membranes of Acholeplasma laidlawii
J. Biol. Chem.
272
929-936
1997
Acholeplasma laidlawii, Acholeplasma laidlawii (Q93P60)
brenda
Li, L.; Storm, P.; Karlsson, O.P.; Berg, S.; Wieslander, A.
Irreversible binding and activity control of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii at an anionic lipid bilayer surface
Biochemistry
42
9677-9686
2003
Acholeplasma laidlawii, Acholeplasma laidlawii (Q93P60)
brenda
Semeniuk, A.; Sohlenkamp, C.; Duda, K.; Hlzl, G.
A bifunctional glycosyltransferase from Agrobacterium tumefaciens synthesizes monoglucosyl and glucuronosyl diacylglycerol under phosphate deprivation
J. Biol. Chem.
289
10104-10114
2014
Agrobacterium tumefaciens (Q7CXE5), Agrobacterium tumefaciens, Agrobacterium tumefaciens ATCC 33970 (Q7CXE5)
brenda
Eriksson, H.M.; Persson, K.; Zhang, S.; Wieslander, K.
High-yield expression and purification of a monotopic membrane glycosyltransferase
Protein Expr. Purif.
66
143-148
2009
Acholeplasma laidlawii (Q93P60)
brenda
Matsuoka, S.; Seki, T.; Matsumoto, K.; Hara, H.
Suppression of abnormal morphology and extracytoplasmic function sigma activity in Bacillus subtilis ugtP mutant cells by expression of heterologous glucolipid synthases from Acholeplasma laidlawii
Biosci. Biotechnol. Biochem.
80
2325-2333
2016
Bacillus subtilis (P54166), Acholeplasma laidlawii (Q93P60), Bacillus subtilis 168 (P54166)
-
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.337)
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