Information on EC 2.7.1.130 - tetraacyldisaccharide 4'-kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.130
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RECOMMENDED NAME
GeneOntology No.
tetraacyldisaccharide 4'-kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + {2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl}-(1->6)-{2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate} = ADP + {2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucosaminyl}-(1->6)-{2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl phosphate}
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
lipid IVA biosynthesis
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lipid A biosynthesis
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Lipopolysaccharide biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
ATP:2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-beta-D-1,6-glucosaminyl-beta-phosphate 4'-O-phosphotransferase
Involved with EC 2.3.1.129 (acyl-[acyl-carrier- protein]---UDP-N-acetylglucosamine O-acyltransferase) and EC 2.4.1.182 (lipid-A-disaccharide synthase) in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Escherichia coli.
CAS REGISTRY NUMBER
COMMENTARY hide
107309-06-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
show the reaction diagram
ATP + 2,3-bis[3-(tetradecanoyl)tetradecanoyl]-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,3,2',3'-tetrakis[3-(tetradecanoyl)tetradecanoyl]-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
show the reaction diagram
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-
-
?
ATP + 2-(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,2',3'-tris(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
show the reaction diagram
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-
-
?
ATP + 2-(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2-(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,2'-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
show the reaction diagram
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-
-
?
ATP + 3-aza-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 3-aza-2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
show the reaction diagram
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-
-
?
CTP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
CDP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
show the reaction diagram
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approx. 50% of activity with ATP
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?
GTP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
GDP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
show the reaction diagram
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approx. 50% of activity with ATP
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?
UTP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
UDP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
show the reaction diagram
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approx. 50% of activity with ATP
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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
ATP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6-)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate
ADP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate
show the reaction diagram
-
involved with EC 2.3.1.129 and 2.4.1.182 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Nonidet P-40
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inactivation by preincubation
octylglucoside
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inactivation by preincubation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cardiolipin
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other phospholipids including phosphatidylethanolamine, phosphatidylserine, phosphatidylcholine and phosphatidylglycerol are not as effective as cardiolipin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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assay procedure
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo- and ADP/Mg2+-bound forms, to a resolution of 1.9 A and 2.2 A, respectively. The enzyme consists of two alpha/beta/alpha sandwich domains connected by a two-stranded beta-sheet linker. The N-terminal domain, which has most structural homology to other family members, is responsible for catalysis at the P-loop and positioning of the disaccharide 1-phosphate substrate for phosphoryl transfer on the inner membrane. The smaller C-terminal domain helps to bind the nucleotide substrate and Mg2+ cation using a 25° hinge motion about its base
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
25% glycerol stabilizes
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phosphoenolpyruvate stabilizes
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression of lipid A 4'-kinase structural gene lpxK in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D138A
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity
D139A
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity
G47A
about 43% of wild-type activity
G48A
about 1.8% of wild-type activity
G50A
about 0.1% of wild-type activity
K51A
about 0.1% of wild-type activity
S53A
about 9.9% of wild-type activity
T52A
about 0.1% of wild-type activity
Show AA Sequence (5738 entries)
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