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Information on EC 5.3.1.28 - D-sedoheptulose 7-phosphate isomerase and Organism(s) Escherichia coli and UniProt Accession P63224

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IUBMB Comments
In Gram-negative bacteria 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-positive bacteria the enzyme is involved in biosynthesis of GDP-D-glycero-alpha-D-manno-heptose, which is required for assembly of S-layer glycoprotein.
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This record set is specific for:
Escherichia coli
UNIPROT: P63224
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
phosphoheptose isomerase, hp0857, sedoheptulose-7-phosphate isomerase, sedoheptulose 7-phosphate isomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoheptose isomerase
-
sedoheptulose-7-phosphate isomerase
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
D-glycero-D-manno-heptose 7-phosphate aldose-ketose-isomerase
In Gram-negative bacteria 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-positive bacteria the enzyme is involved in biosynthesis of GDP-D-glycero-alpha-D-manno-heptose, which is required for assembly of S-layer glycoprotein.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-sedoheptulose 7-phosphate
D-glycero-alpha,beta-D-manno-heptose 7-phosphate
show the reaction diagram
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
show the reaction diagram
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-sedoheptulose 7-phosphate
D-glycero-alpha,beta-D-manno-heptose 7-phosphate
show the reaction diagram
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
show the reaction diagram
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
show the reaction diagram
-
-
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-[(1R)-1-hydroxy-2-(phosphonoamino)ethyl]-D-lyxopyranose
-
-
5-[(1R)-2-[4,5-bis(hydroxymethyl)-1H-1,2,3-triazol-1-yl]-1-hydroxyethyl]-D-lyxopyranose
-
poor inhibitor
5-[(1R,2R)-2-carboxy-1,2-dihydroxyethyl]-D-lyxopyranose
-
-
5-[(1S,2S)-1,2-dihydroxy-2-phosphonoethyl]-D-lyxopyranose
-
-
5-{(1R)-1-hydroxy-2-[(methylsulfonyl)amino]ethyl}-D-lyxopyranose
-
poor inhibitor
methyl 5-[(1R)-1-hydroxy-2-(phosphonooxy)ethyl]-alpha-D-lyxopyranoside
-
-
methyl 5-[(1R)-1-hydroxy-2-(phosphonooxy)ethyl]-alpha-D-xylopyranoside
-
-
methyl 5-[(1R,2R)-2-carboxy-1,2-dihydroxyethyl]-alpha-D-lyxopyranoside
-
poor inhibitor
methyl 5-[(1S)-1-hydroxy-2-(phosphonooxy)ethyl]-alpha-D-lyxopyranoside
-
poor inhibitor
methyl 5-[(1S,2S)-1,2-dihydroxy-2-phosphonoethyl]-alpha-D-lyxopyranoside
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 1.2
D-sedoheptulose 7-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23 - 0.45
D-sedoheptulose 7-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.9
D-sedoheptulose 7-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20600
x * 20600, calculated from sequence
29000
2 * 29000, SDS-PAGE
60000 - 80000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 20600, calculated from sequence
dimer
2 * 29000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structures of GmhA in apo, substrate, and product-bound forms
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D169N
inactive
D94N
kcat/Km for D-sedoheptulose 7-phosphate is 1.8fold higher than wild-type value
H180Q
inactive
H61Q
kcat/Km for D-sedoheptulose 7-phosphate is 2.5fold lower than wild-type value
Q172E
inactive
T120A
inactive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kneidinger, B.; Marolda, C.; Graninger, M.; Zamyatina, A.; McArthur, F.; Kosma, P.; Valvano, M.A.; Messner, P.
Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli
J. Bacteriol.
184
363-369
2002
Aneurinibacillus thermoaerophilus (Q9AGY7), Escherichia coli (P63224)
Manually annotated by BRENDA team
Brooke, J.S.; Valvano, M.A.
Biosynthesis of inner core lipopolysaccharide in enteric bacteria identification and characterization of a conserved phosphoheptose isomerase
J. Biol. Chem.
271
3608-3614
1996
Escherichia coli (P63224), Escherichia coli
Manually annotated by BRENDA team
Taylor, P.L.; Blakely, K.M.; de Leon, G.P.; Walker, J.R.; McArthur, F.; Evdokimova, E.; Zhang, K.; Valvano, M.A.; Wright, G.D.; Junop, M.S.
Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants
J. Biol. Chem.
283
2835-2845
2008
Escherichia coli (P63224), Escherichia coli, Pseudomonas aeruginosa (Q9HVZ0), Pseudomonas aeruginosa
Manually annotated by BRENDA team
Valvano, M.A.; Messner, P.; Kosma, P.
Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides
Microbiology
148
1979-1989
2002
Aneurinibacillus thermoaerophilus (Q9AGY7), Burkholderia mallei (Q9AI36), Burkholderia pseudomallei (Q93UJ2), Campylobacter jejuni (Q9PMN3), Campylobacter jejuni (Q9PNE6), Clostridium acetobutylicum (Q97EQ4), Escherichia coli (P63224), Haemophilus influenzae (P45093), Helicobacter pylori J99 (Q9ZKZ1), Mycobacterium tuberculosis (P9WGG1), Mycobacterium tuberculosis H37Rv (P9WGG1), Neisseria meningitidis (P0A0Y5), Neisseria meningitidis (P0A0Y6), Pseudomonas aeruginosa (Q9HVZ0), Salmonella enterica subsp. enterica serovar Typhimurium (P63223), Vibrio cholerae (Q9KPY2), Yersinia pestis (Q8ZBY7)
Manually annotated by BRENDA team
Durka, M.; Tikad, A.; Perion, R.; Bosco, M.; Andaloussi, M.; Floquet, S.; Malacain, E.; Moreau, F.; Oxoby, M.; Gerusz, V.; Vincent, S.P.
Systematic synthesis of inhibitors of the two first enzymes of the bacterial heptose biosynthetic pathway: towards antivirulence molecules targeting lipopolysaccharide biosynthesis
Chemistry
17
11305-11313
2011
Escherichia coli
Manually annotated by BRENDA team