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Information on EC 2.7.7.38 - 3-deoxy-manno-octulosonate cytidylyltransferase and Organism(s) Escherichia coli and UniProt Accession P42216

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Escherichia coli
UNIPROT: P42216 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cmp-kdo synthetase, 3-deoxy-manno-octulosonate cytidylyltransferase, ctp:cmp-3-deoxy-d-manno-octulosonate cytidylyltransferase, 3-deoxy-d-manno-octulosonate cytidylyltransferase, cmp/kdo synthase, l-cks, cmp:kdo synthase, 2-keto-3-deoxy-d-manno-octulosonate cytidylyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-keto-3-deoxyoctonate cytidylyltransferase
-
-
-
-
3-deoxy-D-manno-octulosonate cytidylyltransferase
CMP-3-deoxy-D-manno-octulosonate pyrophosphorylase
-
-
-
-
CMP-3-deoxy-D-manno-octulosonate synthetase
-
-
-
-
CMP-KDO synthetase
CMP/KDO synthase
-
-
CMP:KDO synthase
-
-
CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase
-
-
-
-
cytidine monophospho-3-deoxy-D-manno-octulosonate pyrophosphorylase
-
-
-
-
cytidine monophospho-3-deoxy-D-manno-octulosonate synthetase
-
-
-
-
K-CKS
-
CKS involved in capsule expression
K-KDO-CT
Kdo cytidylyltransferase
-
L-CKS
-
CKS involved in lipopolysaccharide biosynthesis
L-KDO-CT
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
CTP:3-deoxy-D-manno-octulosonate cytidylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37278-28-7
-
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-deoxy-D-manno-octulosonate
diphosphate + CMP-3-deoxy-D-manno-octulosonate
show the reaction diagram
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
-
-
-
-
r
CTP + 3-deoxy-D-manno-octulosonate
CMP-3-deoxy-D-manno-octulosonate + diphosphate
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
r
CTP + 5-epi-Kdo
diphosphate + CMP-5-epi-3-deoxy-D-manno-octulosonate
show the reaction diagram
-
-
-
-
r
CTP + 5-fluoro-2-keto-3,5-dideoxyoctulosonate
diphosphate + CMP-5-fluoro-2-keto-3,5-dideoxy octulosonate
show the reaction diagram
-
-
-
-
r
CTP + 8-azido-3,8-dideoxy-D-manno-oct-2-ulosonate
diphosphate + CMP-azido-3,8-dideoxy-D-manno-oct-2-ulosonate
show the reaction diagram
the enzyme does not efficiently recognize azido-3,8-dideoxy-D-manno-oct-2-ulosonate as a substrate
-
-
?
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
?
-
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
CTP + 3-deoxy-D-manno-octulosonate
diphosphate + CMP-3-deoxy-D-manno-octulosonate
show the reaction diagram
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
-
monovalent cations Na+, Li+ andK+ are ineffective in stimulating the enzyme, as are divalent cations Hg2+, Ni2+, and Fe2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,4S,5R)-3-[2-[(S)-1-((S)-1-carboxy-ethylcarbamoyl)-ethylamino]-ethyl]-4,5-dihydroxy-cyclohexanecarboxylic acid
-
-
2,6-Anhydro-3-deoxy-D-glycero-D-talo-octanoate
diphosphate
-
weak inhibition
Hg2+
-
strong inhibition
additional information
-
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
2.6
8-azido-3,8-dideoxy-D-manno-oct-2-ulosonate
at pH 7.6, temperature not specified in the publication
-
0.024 - 2.5
CTP
0.34
dCTP
-
pH 8.0, 37°C
0.88
UTP
-
pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.21 - 21.9
3-deoxy-D-manno-octulosonate
1.36
8-azido-3,8-dideoxy-D-manno-oct-2-ulosonate
at pH 7.6, temperature not specified in the publication
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
3-deoxy-D-manno-octulosonate
at pH 7.6, temperature not specified in the publication
0.5
8-azido-3,8-dideoxy-D-manno-oct-2-ulosonate
at pH 7.6, temperature not specified in the publication
-
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
-
K-CKS
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.6
-
0.2 M Tris-acetate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
about half-maximal activity at pH 7.0 and pH 8.4
7.5 - 10.2
-
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
-
about half-maximal activity at pH 7.5 and about 60% of maximal activity at pH 10.5 in glycine-NaOH buffer
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.7
-
K-CKS, isolectric capillary electrophoresis
4
-
isoelectric focusing
4.15 - 4.4
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KPSU5_ECOLX
246
0
27159
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
recombinant KpsU protein, K-CKS, SDS-PAGE
27030
calculated from cDNA
28000
-
gel filtration, SDS-PAGE
35000
-
molecular sieving
35000 - 40000
-
SDS-PAGE
35000 - 45000
-
sucrose density gradient centrifugation
36000
-
1 * 36000, SDS-PAGE
40000 - 46000
-
gel filtration
44000
-
sucrose density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 36000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized in space group P2(1), cell dimensions a = 46.1, b = 133.8, c = 48.5, beta 102.6°
KDO-CT crystallized in presence of CMP-NeuAc, crystallizes as a dimer composed of 27kDa monomers
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 8
-
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
-
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
-
-20°C,partially purified enzyme relatively stable, approximately 20% of the activity is lost after storage for 1 year
-
-90°C, partially purified protein, 0.05 M potassium phosphate buffer, 0.5 mM dithiothreitol, stable for up to 3 months
-
-90°C, purified protein, 0.05 M potassium phosphate buffer, 0.5 mM dithiothreitol, no loss detected for up to 4 months
-
4°C, partially purified enzyme, no loss of activity for up to 1 month
-
4°C, partially purified protein, 0.05 M potassium phosphate buffer, 0.5 mM dithiothreitol, stable for up to 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
-
recombinant KpsU protein, K-CKS
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
gene amplified from Escherichia coli K-235 DNA cloned and overexpressed in recombinant Escherichia coli
-
kps gene cluster cloned and sequenced, K-CKS overexpressed in recombinant Escherichia coli JA221 (pCR3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ghalambor, M.A.; Heath, E.H.
The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. IV. Purification and properties of cytidine monophosphate 3-deoxy-D-manno-octulosonate synthetase
J. Biol. Chem.
241
3216-3221
1966
Escherichia coli, Escherichia coli 0111-B4
Manually annotated by BRENDA team
Ray, P.H.; Benedict, C.D.; Grasmuk, H.
Purification and characterization of cytidine 5-triphosphate:cytidine 5-monophosphate-3-deoxy-D-manno-octulosonate cytidylyltransferase
J. Bacteriol.
145
1273-1280
1981
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
Ray, P.H.; Benedict, C.D.
CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase)
Methods Enzymol.
83
535-540
1982
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
Claesson, A.; Luthman, K.; Gustafsson, K.; Bondesson, G.
A 2-deoxy analogue of KDO as the first inhibitor of the enzyme CMP-KDO synthetase
Biochem. Biophys. Res. Commun.
143
1063-1068
1987
Escherichia coli, Escherichia coli D21, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium SL 1102
Manually annotated by BRENDA team
Rosenow, C.; Roberts, I.S.; Jann, K.
Isolation from recombinant Escherichia coli and characterization of CMP-Kdo synthetase, involved in the expression of the capsular K5 polysaccharide (K-CKS)
FEMS Microbiol. Lett.
125
159-164
1995
Escherichia coli
Manually annotated by BRENDA team
Sugai, T.; Lin, C.H.; Shen, G.J.; Wong, C.H.
CMP-KDO synthetase: overproduction and application to the synthesis of CMP-KDO and analogs
Bioorg. Med. Chem.
3
313-320
1995
Escherichia coli
Manually annotated by BRENDA team
Jelakovic, S.; Jann, K.; Schulz, G.E.
The three-dimensional structure of capsule-specific CMP: 2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli
FEBS Lett.
391
157-161
1996
Escherichia coli
Manually annotated by BRENDA team
Royo, J.; Gomez, E.; Hueros, G.
CMP-KDO synthetase. A plant gene borrowed from Gram-negative eubacteria
Trends Genet.
16
432-433
2000
Aggregatibacter actinomycetemcomitans, Aquifex pyrophilus, Arabidopsis thaliana, Chlamydia pneumoniae, Chlamydia trachomatis, Chlorobaculum tepidum, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Neisseria meningitidis, no activity in Caenorhabditis elegans, no activity in Drosophila melanogaster, no activity in Saccharomyces cerevisiae, Rickettsia prowazekii, Solanum lycopersicum, Vibrio cholerae serotype O1, Yersinia pestis, Zea mays
Manually annotated by BRENDA team
Jelakovic, S.; Schulz, G.E.
The structure of CMP:2-keto-3-deoxy-manno-octonic acid synthetase and of its complexes with substrates and substrate analogs
J. Mol. Biol.
312
143-155
2001
Escherichia coli, Escherichia coli (P42216)
Manually annotated by BRENDA team
Bravo, I.G.; Reglero, A.
The cytidyltransferases family: Properties, kinetics, genomic and phylogeny
Recent Res. Devel. Biochem.
4
224-254
2003
Aquifex aeolicus, Arabidopsis thaliana (Q9C920), Caulobacter vibrioides (Q9A4A3), Chlamydia muridarum, Chlamydia pneumoniae, Chlamydia trachomatis, Escherichia coli, Escherichia coli (P42216), Haemophilus influenzae, Helicobacter pylori, Mesorhizobium loti (Q98BN3), Neisseria meningitidis, Neisseria meningitidis (Q9K0D6), Neisseria meningitidis MC58 (Q9K0D6), Pasteurella multocida, Pseudomonas aeruginosa, Rickettsia conorii (Q92I96), Rickettsia prowazekii, Salmonella enterica subsp. enterica serovar Typhimurium, Sinorhizobium meliloti (Q92SX6), Vibrio cholerae (Q9KQX2), Xylella fastidiosa (Q9PB46), Zea mays, Zea mays (Q9M4D3), Zea mays (Q9M4G3)
-
Manually annotated by BRENDA team
Kondo, K.; Doi, H.; Adachi, H.; Nishimura, Y.
Synergistic effect of CMP/KDO synthase inhibitors with antimicrobial agents on inhibition of production and release of vero toxin by enterohaemorrhagic Escherichia coli O157:H7
Bioorg. Med. Chem. Lett.
14
467-470
2004
Escherichia coli
Manually annotated by BRENDA team
Yi, L.; Velasquez, M.S.; Holler, T.P.; Woodard, R.W.
A simple assay for 3-deoxy-D-manno-octulosonate cytidylyltransferase and its use as a pathway screen
Anal. Biochem.
416
152-158
2011
Escherichia coli
Manually annotated by BRENDA team
Wen, L.; Zheng, Y.; Li, T.; Wang, P.G.
Enzymatic synthesis of 3-deoxy-D-manno-octulosonic acid (KDO) and its application for LPS assembly
Bioorg. Med. Chem. Lett.
26
2825-2828
2016
Escherichia coli (P04951)
Manually annotated by BRENDA team
Nilsson, I.; Grove, K.; Dovala, D.; Uehara, T.; Lapointe, G.; Six, D.A.
Molecular characterization and verification of azido-3,8-dideoxy-D-manno-oct-2-ulosonic acid incorporation into bacterial lipopolysaccharide
J. Biol. Chem.
292
19840-19848
2017
Escherichia coli (P04951)
Manually annotated by BRENDA team