Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.5.1.55 - 3-deoxy-8-phosphooctulonate synthase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9ZFK4

for references in articles please use BRENDA:EC2.5.1.55
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q9ZFK4 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
kdo8ps, kdo8p synthase, kdo 8-p synthase, 3-deoxy-d-manno-octulosonate 8-phosphate synthase, kdo-8-p synthase, kdops, kdo-8-phosphate synthetase, atkdsa1, 3-deoxy-d-manno-octulosonate-8-phosphate synthase, 3-deoxy-d-manno-octulosonic acid 8-phosphate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating)
-
-
-
-
2-dehydro-3-deoxyphosphooctonate aldolase
2-keto-3-deoxy-8-phosphooctonic acid synthetase
-
-
-
-
2-keto-3-deoxy-8-phosphooctonic synthetase
-
-
-
-
2-keto-3-deoxy-D-manno-octulosonate-8-phosphate synthase
-
-
3-deoxy-D-manno-octulosonate 8-phosphate synthetase
-
-
-
-
3-deoxy-D-manno-octulosonate-8-phosphate synthase
-
-
-
-
3-deoxy-D-manno-octulosonic acid 8-phosphate synthase
-
-
-
-
3-deoxy-D-mannooctulosonate-8-phosphate synthetase
-
-
-
-
3-deoxyoctulosonic 8-phosphate synthetase
-
-
-
-
8-phospho-2-dehydro-3-deoxy-D-octonate D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating)
-
-
-
-
aldolase, phospho-2-keto-3-deoxyoctonate
-
-
-
-
KDO-8-P synthase
-
-
-
-
KDO-8-P synthetase
-
-
-
-
KDO8-P
-
-
-
-
Kdo8P synthase
-
-
-
-
KDO8PS
KDOPS
-
-
-
-
KDPO synthetase
-
-
-
-
KdsA
-
-
-
-
Phospho-2-dehydro-3-deoxyoctonate aldolase
-
-
-
-
phospho-2-keto-3-deoxyoctonate aldolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:D-arabinose-5-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-96-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
show the reaction diagram
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
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
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
-
1 mM, 22% inhibition
Cu2+
-
1 mM, 80% inhibition
Fe2+
-
1 mM, 30% inhibition
Mn2+
-
1 mM, 40% inhibition
Zn2+
-
1 mM, 34% inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1 - 9
-
pH 6.1: about 35% of maximal activity, pH 9.0: about 25% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme catalyzes a key step in the synthesis of the lipopolysaccharide of most Gram-negative bacteria, it catalyzes the condensation reaction between phosphoenolpyruvate and arabinose 5-phosphate to produce 3-deoxy-D-manno-octulosonate 8-phosphate. The enzyme is vital for for proper synthesis and assembly of lipoplysaccharides and the survival and virulence of Pseudomonas aeruginosa
additional information
-
active site structure, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
-
the enzyme structure is a prototypical alpha/beta TIM barrel structure expected from this family of enzymes and contains a tetramer in the asymmetric unit
additional information
-
two-dimensional structure comparison
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged enzyme, sitting drop vapour diffusion method, mixing of 0.003 ml of 5 mg/ml protein in 0.2 M Tris-HCl, pH 7.4, 0.1 M NaCl, 0.05% 2-mercaptoethanol, and 0.1 mM phosphoenolpyruvate with 0.0015 ml of reservoir solution containing 0.2 M calcium acetate, 0.1 M sodium cacodylate, pH 6.5, 18% w/v PEG 8000, 20°C, 2 days, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacementusing structure PDB ID 1g7v and model building
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against 0.01 M Tris-HCl, pH 7.5, containing 0.01 M thioglycerol for 4 h, less than 20% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta2 (pLysS) DE3 by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene kdo8ps, recombinant expression of His6-tagged codon-optimized enzyme in Escherichia coli strain Rosetta2 (pLysS) DE3
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Levin, D.H.; Racker, E.
Condensation of arabinose 5-phosphate and phosphorylenol pyruvate by 2-keto-3-deoxy-8-phosphooctonic acid synthetase
J. Biol. Chem.
234
2532-2539
1959
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Levin, D.H.; Racker, E.
2-Keto-3-deoxy-8-phosphooctonic acid synthetase
Methods Enzymol.
8
216-221
1966
Pseudomonas aeruginosa
-
Manually annotated by BRENDA team
Birck, M.R.; Woodard, R.W.
Aquifex aeolicus 3-Deoxy-D-manno-2-octulosonic acid 8-phosphate synthase: A new class of KDO 8-P synthase?
J. Mol. Evol.
52
205-214
2001
Actinobacillus pleuropneumoniae (O68662), Aggregatibacter actinomycetemcomitans, Aquifex aeolicus, Aquifex aeolicus (O66496), Arabidopsis thaliana, Bordetella bronchiseptica, Bordetella pertussis, Campylobacter jejuni, Caulobacter vibrioides, Chlamydia pneumoniae (Q9Z7I4), Chlamydia psittaci (Q46225), Chlamydia trachomatis (P0CD74), Chlorobaculum tepidum, Escherichia coli (P0A715), Escherichia coli, Haemophilus influenzae (P45251), Helicobacter pylori, Helicobacter pylori (Q9ZN55), Klebsiella pneumoniae, Mannheimia haemolytica (P95514), Neisseria gonorrhoeae (Q9XB02), Neisseria meningitidis (Q9XAZ3), Pasteurella multocida, Pisum sativum, Porphyromonas gingivalis, Pseudomonas aeruginosa (Q9ZFK4), Rickettsia prowazekii (Q9ZE84), Salmonella enterica subsp. enterica serovar Typhi, Shewanella putrefaciens, Vibrio cholerae serotype O1, Yersinia pestis
Manually annotated by BRENDA team
Nelson, S.K.; Kelleher, A.; Robinson, G.; Reiling, S.; Asojo, O.A.
Structure of 2-keto-3-deoxy-D-manno-octulosonate-8-phosphate synthase from Pseudomonas aeruginosa
Acta Crystallogr. Sect. F
69
1084-1088
2013
Pseudomonas aeruginosa
Manually annotated by BRENDA team