Information on EC 2.7.1.167 - D-glycero-beta-D-manno-heptose-7-phosphate kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.167
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RECOMMENDED NAME
GeneOntology No.
D-glycero-beta-D-manno-heptose-7-phosphate kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glycero-beta-D-manno-heptose 7-phosphate + ATP = D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ADP-L-glycero-beta-D-manno-heptose biosynthesis
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Lipopolysaccharide biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-glycero-beta-D-manno-heptose 7-phosphate 1-phosphotransferase
The bifunctional protein hldE includes D-glycero-beta-D-manno-heptose-7-phosphate kinase and D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase activity (cf. EC 2.7.7.70). The enzyme is involved in biosynthesis of ADP-L-glycero-beta-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria. The enzyme selectively produces D-glycero-beta-D-manno-heptose 1,7-bisphosphate [5].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional protein hldE includes: D-beta-D-heptose 7-phosphate kinase and D-beta-D-heptose 1-phosphate adenosyltransferase
SwissProt
Manually annotated by BRENDA team
bifunctional protein hldE includes: D-beta-D-heptose 7-phosphate kinase and D-beta-D-heptose 1-phosphate adenosyltransferase
SwissProt
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
7-O-phosphono-6-deoxy-glycero-D-manno-heptopyranosyl phosphate + ATP
? + ADP
show the reaction diagram
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low activity
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-
?
7-phosphate-D-glycero-beta-D-manno-heptose + ATP
D-glycero-D-manno-beta-heptose 1,7-bisphosphate + ADP
show the reaction diagram
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-
-
-
?
D-glycero-beta-D-manno-heptose 7-phosphate + ATP
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP
show the reaction diagram
D-glycero-D-manno-heptose 7-phosphate + ATP
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP
show the reaction diagram
D-glycero-D-manno-heptose 7-phosphate + ATP
D-glycero-beta-D-mannoheptose 1,7-bisphosphate + ADP
show the reaction diagram
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
D-glycero-D-manno-heptose 7-phosphate + ATP
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP
show the reaction diagram
D-glycero-D-manno-heptose 7-phosphate + ATP
D-glycero-beta-D-mannoheptose 1,7-bisphosphate + ADP
show the reaction diagram
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-
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[[2-([[5-(2,6-dichlorophenyl)-1,2,4-triazin-3-yl]amino]methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid
binds to the nucleotide-binding sites without altering the overall structure of the enzyme or interfering with the binding of D-glycero-beta-D-manno-heptose-7-phosphate
[[2-([[5-(2,6-dimethoxyphenyl)-1,2,4-triazin-3-yl]amino]methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid
binds to the nucleotide-binding sites without altering the overall structure of the enzyme or interfering with the binding of D-glycero-beta-D-manno-heptose-7-phosphate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00023
[[2-([[5-(2,6-dichlorophenyl)-1,2,4-triazin-3-yl]amino]methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid
Burkholderia cepacia;
B4EB35
pH not specified in the publication, temperature not specified in the publication
0.00081
[[2-([[5-(2,6-dimethoxyphenyl)-1,2,4-triazin-3-yl]amino]methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid
Burkholderia cepacia;
B4EB35
pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
PDB
SCOP
CATH
UNIPROT
ORGANISM
Burkholderia pseudomallei (strain K96243);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
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x * 53000, calculated from sequence
55000
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x * 55000, SDS-PAGE
83000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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HldE comprises two functional domains: an N-terminal region with homology to the ribokinase superfamily (HldE1 domain) and a C-terminal region with homology to the cytidylyltransferase superfamily. HldE functional unit is a dimer and structural components present in each HldE1 monomer are required for enzymatic activity
additional information
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the N-terminal domain I spans amino acids 1-318 and shares structural features with members of the ribokinase family. The C-terminal domain II, which spans amino acids 344-477, has all the conserved features of the cytidylyltransferase superfamily
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of enzyme-substrate and enzyme-product complexes and complexes with inhibitors [[2-({[5-(2,6-dimethoxyphenyl)-1,2,4-triazin-3-yl]amino}methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid and [[2-([[5-(2,6-dichlorophenyl)-1,2,4-triazin-3-yl]amino]methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid. Enzyme HldA is structurally similar to members of the PfkB carbohydrate kinase family and appears to catalyze heptose phosphorylation via an in-line mechanism mediated mainly by a conserved aspartate, Asp270. Both inhibitors adopt a folded conformation and occupy the nucleotide-binding sites
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
the rfaE gene encodes a polypeptide of 477 amino acid residues highly homologous to the Salmonella enterica rfaE protein (98% identity), Escherichia coli (93% identity), Yersenia pestis (85% identity), Haemophilus influenzae (70% identity) and Helicobacter pyroli (41% identity)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D264E
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loss of activity
D264N
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loss of enzymatic activity in the mutant protein is not caused by drastic alterations in protein structure
E198D
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loss of enzymatic activity in the mutant protein is not caused by drastic alterations in protein structure
N195D
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loss of activity
additional information
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development of an efficient one-pot three enzymes strategy for chemoenzymatic synthesis of ADP-D-glycero-beta-D-manno-heptose (ADP-D, D-heptose) using chemically synthesized D,D-heptose-7-phosphate and the ADP-D,D-heptose biosynthetic enzymes HldE and GmhB, method, overview
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