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Information on EC 2.4.1.337 - 1,2-diacylglycerol 3-alpha-glucosyltransferase
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EC Tree
2.4.1.337 1,2-diacylglycerol 3-alpha-glucosyltransferaseIUBMB 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.
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Word Map
- 2.4.1.337
- laidlawii
-
bilayer
- acholeplasma
-
curvature
-
nonbilayer-prone
- phospholipids
- phosphatidylglycerol
-
nonbilayer
- liposome
-
zwitterionic
-
liquid-crystalline
- lactose
-
permease
- phosphatidylethanolamine
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
alpha-monoglucosyldiacylglycerol synthase, Atu2297, MGlcDAG synthase, 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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Atu2297
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
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
-
-
-
?
UDP-alpha-D-glucose + 1,2-dipalmitoyl-sn-glycerol
UDP + 1,2-dipalmitoyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
-
-
-
?
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
-
-
-
?
UDPglucose + 1,2-dipalmitoylglycerol
UDP + 3-D-glucosyl-1,2-dipalmitoylglycerol
twice as high enzyme activity as sn-1,2-dioleoylglycerol at all concentrations up to 2.5 mol% concentration
-
-
?
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-glucose + a 1,2-diacyl-sn-glycerol
UDP + a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
Agrobacterium tumefaciens ATCC 33970
-
-
-
?
UDP-alpha-D-glucuronic acid + a 1,2-diacyl-sn-glycerol
UDP + a 1,2-diacyl-3-O-(alpha-D-glucuronosyl)-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
Agrobacterium tumefaciens ATCC 33970
-
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
-
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
-
-
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
-
-
-
?
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
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
-
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
the product monoglucosyldiacylglycerol is the first glucolipid along the glucolipid pathway, and a major nonbilayer-prone lipid in the single membrane
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
promiscuous glycosyltransferase, usues UDP-glucose or UDP-glucuronic acid as sugar donors
-
-
?
additional information
?
-
-
promiscuous glycosyltransferase, usues UDP-glucose or UDP-glucuronic acid as sugar donors
-
-
?
additional information
?
-
Agrobacterium tumefaciens ATCC 33970
promiscuous glycosyltransferase, usues UDP-glucose or UDP-glucuronic acid as sugar donors
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
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
-
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
the product monoglucosyldiacylglycerol is the first glucolipid along the glucolipid pathway, and a major nonbilayer-prone lipid in the single membrane
-
-
?
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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
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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
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
-
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
-
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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
-
A0A5J4F6T9_MICAE
408
0
45807
TrEMBL
-
A0A494WPE4_CLOS5
Clostridium scindens (strain ATCC 35704 / DSM 5676 / VPI 13733 / 19)
422
0
48353
TrEMBL
-
A0A346BDV4_9BURK
391
0
41761
TrEMBL
-
A0A645BAP6_9ZZZZ
391
0
44373
TrEMBL
other Location (Reliability: 2)
A0A644T0V4_9ZZZZ
391
0
44666
TrEMBL
other Location (Reliability: 4)
A0A644WZM4_9ZZZZ
406
0
46060
TrEMBL
Secretory Pathway (Reliability: 4)
A0A543Q2K1_ACITH
392
0
43976
TrEMBL
-
A0A645IEX2_9ZZZZ
125
0
14110
TrEMBL
other Location (Reliability: 1)
A0A645BK63_9ZZZZ
205
0
23229
TrEMBL
other Location (Reliability: 1)
A0A645CFW2_9ZZZZ
207
0
23180
TrEMBL
other Location (Reliability: 2)
A0A644Z5A2_9ZZZZ
385
0
44238
TrEMBL
other Location (Reliability: 2)
A0A645AHF4_9ZZZZ
415
0
46516
TrEMBL
Mitochondrion (Reliability: 3)
A0A7W8CXH3_9FIRM
659
0
76040
TrEMBL
-
A0A399F897_9DEIN
400
0
45124
TrEMBL
-
A0A645G8Y6_9ZZZZ
151
0
16848
TrEMBL
other Location (Reliability: 2)
A0A644YLH6_9ZZZZ
382
0
42793
TrEMBL
other Location (Reliability: 3)
A0A644YLK8_9ZZZZ
385
0
44140
TrEMBL
other Location (Reliability: 2)
A0A645CCL0_9ZZZZ
396
0
44559
TrEMBL
other Location (Reliability: 4)
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.; Hölzl, 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
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