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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-
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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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?
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
ORGANISM
UNIPROT
Burkholderia pseudomallei (strain K96243)
Burkholderia pseudomallei (strain K96243)
Burkholderia pseudomallei (strain K96243)
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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