Information on EC 2.4.1.336 - monoglucosyldiacylglycerol synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.4.1.336
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RECOMMENDED NAME
GeneOntology No.
monoglucosyldiacylglycerol synthase
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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-(beta-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
galactolipid biosynthesis II
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Glycerolipid metabolism
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Metabolic pathways
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type I lipoteichoic acid biosynthesis (S. aureus)
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SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:1,2-diacyl-sn-glycerol 3-beta-D-glucosyltransferase
The enzymes from cyanobacteria are involved in the biosynthesis of galactolipids found in their photosynthetic membranes. The enzyme belongs to the GT2 family of configuration-inverting glycosyltranferases [2]. cf. EC 2.4.1.337, 1,2-diacylglycerol 3-alpha-glucosyltransferase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
gene sll1377
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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-dipalmitoyl-sn-glycerol
UDP + 1,2-dipalmitoyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
UDP-alpha-D-glucose + 1-oleoyl-2-palmitoyl-sn-glycerol
UDP + 1-oleoyl-2-palmitoyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
UDP-glucose + 1,2-diacyl-sn-glycerol
UDP + 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
UDPglucose + 1,2-diacylglycerol
UDP + 3-D-glucosyl-1,2-diacylglycerol
show the reaction diagram
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?
UDPglucose + 1,2-dipalmitoylglycerol
UDP + 3-D-glucosyl-1,2-dipalmitoylglycerol
show the reaction diagram
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?
UDPglucose + 1-oleoyl-2-palmitoylglycerol
UDP + 3-D-glucosyl-1-oleoyl-2-palmitoylglycerol
show the reaction diagram
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?
UDPglucose + 1-stearoyl-2-palmitoylglycerol
UDP + 3-D-glucosyl-1-stearoyl-2-palmitoylglycerol
show the reaction diagram
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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
UDP-alpha-D-glucose + 1,2-dipalmitoyl-sn-glycerol
UDP + 1,2-dipalmitoyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
UDP-alpha-D-glucose + 1-oleoyl-2-palmitoyl-sn-glycerol
UDP + 1-oleoyl-2-palmitoyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
UDP-glucose + 1,2-diacyl-sn-glycerol
UDP + 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
digalactosyldiacylglycerol
; inhibition by the final products of galactolipid synthesis
monogalactosyldiacylglycerol
; inhibition by the final products of galactolipid synthesis
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sulfoquinovosyldiacylglycerol
7fold stimulation by 40 mol% in mixed micelles; potently stimulates the enzyme activity
additional information
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isoform Sll1377 shows temperature-dependent activation, whereas the Sll1377 protein level remains unchanged
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
UDPglucose
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.7
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pH 5.0: about 45% of maximal activity, pH 8.7: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28 - 55
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28C: 50% of maximal activity, 55C: 35% of maximal activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structural model displays the characteristic double Rossmann fold of the GT-B superfamily, with the active site located in the cleft between the two domains. The C-terminal tail stretches back to and interacts with the N domain, perhaps acting as a tether that maintains close contacts between the two domains
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, stable for at least 2 months, crude enzyme extract
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from membranes fraction by ultracentrifugation
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli; recombinant overexpression in Escherichia coli strain BL21-AI membranes resulting in an upregulated phospholipid synthesis and vesiculation, acyl chain ordering of lipids during enzyme MGS production, overview
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expression in Synechocystis sp.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K67A/R70A
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mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles
K67A/R70A/R83A/K84A
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mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles
K76A/R77A
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mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles
L62A/V63A/V66A
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mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles
R63A/K64A
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mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles
R80A/K81A
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mutation in the binding alpha helix, mutant is active and able to generate internal vesicles.
R83A/K84A
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mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles; mutation in the binding alpha helix, mutant is active and able to generate internal vesicles
D147Q
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mutation significantly reduces the activity and blocks temperature-dependent activation
D200A
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mutation significantly reduces the activity and blocks temperature-dependent activation
R329A
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mutation significantly reduces the activity and blocks temperature-dependent activation
R331A
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mutation significantly reduces the activity and blocks temperature-dependent activation
additional information
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deletion of 9, 19 or 29 amino acids of the C-terminal tail destroys the activity in vitro. The ability to generate internal vesicles is dirupted in mutants lacking 19 and 29 amino acids