Information on EC 2.7.7.38 - 3-deoxy-manno-octulosonate cytidylyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.7.7.38
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RECOMMENDED NAME
GeneOntology No.
3-deoxy-manno-octulosonate cytidylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CTP + 3-deoxy-D-manno-octulosonate = diphosphate + CMP-3-deoxy-D-manno-octulosonate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
CMP-3-deoxy-D-manno-octulosonate biosynthesis
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Lipopolysaccharide biosynthesis
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Metabolic pathways
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CMP-KDO biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
CTP:3-deoxy-D-manno-octulosonate cytidylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
37278-28-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
strain 0111-B4
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Manually annotated by BRENDA team
strain D21
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Manually annotated by BRENDA team
strain K12
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Manually annotated by BRENDA team
CSK gene in partial release of human chromosome 5; CSK gene in partial release of human chromosome 7
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-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
strain B
SwissProt
Manually annotated by BRENDA team
no activity in Caenorhabditis elegans
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-
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Manually annotated by BRENDA team
no activity in Drosophila melanogaster
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-
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Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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mutation of the KDO gene renders pollen infertile through the inhibition of pollen tube elongation. Results suggest that KDO is an indispensable component of RG-II, and that the complete B-RG-II complex is essential for the cell wall integrity of rapidly growing tissues
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + 3,5-dideoxy-5-fluoro-beta-D-manno-2-octulopyranosonic acid
diphosphate + CMP-3,5-dideoxy-5-fluoro-beta-D-manno-2-octulopyranosonic acid
show the reaction diagram
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-
-
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r
CTP + 3-deoxy-D-manno-octulosonate
CMP-3-deoxy-D-manno-octulosonate + diphosphate
show the reaction diagram
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-
-
-
?
CTP + 3-deoxy-D-manno-octulosonate
diphosphate + CMP-3-deoxy-D-manno-octulosonate
show the reaction diagram
CTP + 5-deoxy-Kdo
diphosphate + CMP-5-deoxy-3-deoxy-D-manno-octulosonate
show the reaction diagram
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-
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r
CTP + 5-epi-Kdo
diphosphate + CMP-5-epi-3-deoxy-D-manno-octulosonate
show the reaction diagram
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-
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r
CTP + 5-fluoro-2-keto-3,5-dideoxyoctulosonate
diphosphate + CMP-5-fluoro-2-keto-3,5-dideoxy octulosonate
show the reaction diagram
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-
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r
dCTP + 3-deoxy-D-manno-octulosonate
diphosphate + dCMP-3-deoxy-D-manno-octulosonate
show the reaction diagram
UTP + 3-deoxy-D-manno-octulosonate
diphosphate + UMP-3-deoxy-D-manno-octulosonate
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
CTP + 3-deoxy-D-manno-octulosonate
diphosphate + CMP-3-deoxy-D-manno-octulosonate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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monovalent cations Na+, Li+ andK+ are ineffective in stimulating the enzyme, as are divalent cations Hg2+, Ni2+, and Fe2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,4S,5R)-3-[2-[(S)-1-((S)-1-carboxy-ethylcarbamoyl)-ethylamino]-ethyl]-4,5-dihydroxy-cyclohexanecarboxylic acid
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2,6-Anhydro-3-deoxy-D-glycero-D-talo-octanoate
diphosphate
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weak inhibition
Hg2+
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strong inhibition
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28 - 2
3-deoxy-D-manno-octulosonate
0.024 - 2.5
CTP
0.34
dCTP
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pH 8.0, 37°C
0.88
UTP
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pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.5 - 21.9
3-deoxy-D-manno-octulosonate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0039
2,6-Anhydro-3-deoxy-D-glycero-D-talo-octanoate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3300
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K-CKS
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.3 - 9.6
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9.6
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0.2 M Tris-acetate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
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about half-maximal activity at pH 7.0 and pH 8.4
7.5 - 10.2
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about half-maximal activity at pH 7.5 and about 80% of maximal activity at pH 10.2 in Tris-acetate buffer
7.5 - 10.5
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about half-maximal activity at pH 7.5 and about 60% of maximal activity at pH 10.5 in glycine-NaOH buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.7
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K-CKS, isolectric capillary electrophoresis
4
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isoelectric focusing
4.15 - 4.4
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isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)
Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)
Aquifex aeolicus (strain VF5)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27030
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calculated from cDNA
28000
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gel filtration, SDS-PAGE
29000
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calculated from cDNA
35000 - 40000
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SDS-PAGE
35000 - 45000
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sucrose density gradient centrifugation
35000
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molecular sieving
36000
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1 * 36000, SDS-PAGE
40000 - 46000
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gel filtration
44000
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sucrose density gradient centrifugation
53000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 36000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.1 A resolution. Two Mg2+ ions are part of the active site of the enzyme
crystallized in space group P2(1), cell dimensions a = 46.1, b = 133.8, c = 48.5, beta 102.6°
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KDO-CT crystallized in presence of CMP-NeuAc, crystallizes as a dimer composed of 27kDa monomers
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native crystals are orthorhombic, belonging to space group P2(1)2(1)2(1) with unit-cell parameters a = 48.6, b = 83.1, c = 117.3 A
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the structure of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae complexed with the substrate 3-deoxy-manno-octulosonate is determined at 2.30 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 8
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stable during purification in Tris-acetate or Tris-chloride buffer, more stable in phosphate buffer than in Tris-acetate or Tris-chloride buffer
645227
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freezing and thawing results in substantial loss in activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-1°C, enzyme preparation is most satisfactorily stored since inactivation of the enzyme under this condition is negligible over a period of several months
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-20°C,partially purified enzyme relatively stable, approximately 20% of the activity is lost after storage for 1 year
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-90°C, partially purified protein, 0.05 M potassium phosphate buffer, 0.5 mM dithiothreitol, stable for up to 3 months
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-90°C, purified protein, 0.05 M potassium phosphate buffer, 0.5 mM dithiothreitol, no loss detected for up to 4 months
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4°C, partially purified enzyme, no loss of activity for up to 1 month
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4°C, partially purified protein, 0.05 M potassium phosphate buffer, 0.5 mM dithiothreitol, stable for up to 3 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
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recombinant KpsU protein, K-CKS
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recombinant protein, expressed in Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; ksdB gene cloned by functional complementation of Salmonella typhimurium mutant RG105 and expressed in Escherichia coli
CKS gene in partial release of human chromosome 5, most probably of bacterial origin, 100% identical at the nucleotide level to the Escherichia coli kdsB gene; CKS gene in partial release of human chromosome 7, most probably of bacterial origin, 100% identical at the nucleotide level to the Escherichia coli kdsB gene
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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gene amplified from Escherichia coli K-235 DNA cloned and overexpressed in recombinant Escherichia coli
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kps gene cluster cloned and sequenced, K-CKS overexpressed in recombinant Escherichia coli JA221 (pCR3)
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KpsF cloned in Escherichia coli DH5alpha, overexpressed in Escherichia coli BLR21(DE3)pLysS
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maize gene can complement kdsB Salmonella typhimurium mutant defective in cell wall synthesis
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overexpressed with a C-terminal hexahistidine tag in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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CMP-KDO synthetase inhibitors attract great interest owing to their potential as selective bactericides
analysis
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adaptation of a simple colorimetric assay for diphosphate to the enzyme 3-deoxy-D-manno-octulosonate cytidylyltransferase. This assay can be combined with the malachite green assay for phosphate to form an assay system capable of determining phosphate and diphosphate in the same solution. The assay system has the potential for simultaneous screening of the 3-deoxy-D-manno-octulosonate biosynthesis pathway
medicine
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