Information on EC 3.5.4.30 - dCTP deaminase (dUMP-forming)

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

EC NUMBER
COMMENTARY hide
3.5.4.30
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RECOMMENDED NAME
GeneOntology No.
dCTP deaminase (dUMP-forming)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dCTP + 2 H2O = dUMP + diphosphate + NH3
show the reaction diagram
highly specific; Requires Mg2+. Is highly specific for dCTP as substrate as dCMP, CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated. While most bacteria require two enzymes to form dUMP from dCTP, EC 3.5.4.13, dCTP deaminase and EC 3.6.1.23, dUTP diphosphatase. The archaeon Methanocaldococcus jannaschii uses a single enzyme to carry out both functions. This enzyme can also act as a dUTP diphosphatase, but more slowly
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of amidines
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyrimidine deoxyribonucleotides de novo biosynthesis IV
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Pyrimidine metabolism
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pyrimidine metabolism
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SYSTEMATIC NAME
IUBMB Comments
dCTP aminohydrolase (dUMP-forming)
Requires Mg2+. Is highly specific for dCTP as substrate as dCMP, CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated. While most bacteria require two enzymes to form dUMP from dCTP (EC 3.5.4.13, dCTP deaminase and EC 3.6.1.23, dUTP diphosphatase), the archaeon Methanocaldococcus jannaschii uses a single enzyme to carry out both functions. This enzyme can also act as a dUTP diphosphatase, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-18-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
strain K12
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Manually annotated by BRENDA team
strain K12
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the bifunctional dCTP deaminase-dUTPase coordinates the deamination and triphosphate cleavage reactions
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dCTP + H2O
dUMP + diphosphate + NH3
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
dCTP + H2O
dUMP + diphosphate + NH3
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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dependent on, optimal concentration: 2-5 mM
NaCl
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maximum activity at 0.15 or 2 M
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha,beta-imido-dUTP
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dUTP
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80% inhibition at 1 mM
phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17.6
dCTP
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60°C, pH 7.5
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 - 9
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50% activity at pH 6 and pH 9
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
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SDS-PAGE
77900
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enzyme with addition of six histidines at the N-terminus, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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two trimers can assemble into a hexamer by stacking on top of each other
homotrimer
trimer
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two trimers can assemble into a hexamer by stacking on top of each other
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with dTTP, hanging drop vapor diffusion method, using 200 mM lithium citrate and 20% (w/v) polyethylene glycol 4000
in complex with dCTP and Mg2+
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apo form complexed with dCTP and dUTP, hanging drop vapor diffusion method
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hanging drop vapor diffusion technique, the crystal structure is determined to 1.88 A resolution
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mutant enzyme E145A in complex with the substrate analogue alpha,beta-imido-dUTP and mutant enzyme E145Q in complex with diphosphate, hanging drop vapor diffusion method, using 0.2 M potassium citrate (E135Q) or 0.2 M potassium hydrogen phosphate (E145A) and 20% (w/v) PEG3350
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
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thermostable, loss of 30% activity after 10 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation 60%, DEAE 52, pH 6.8
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ammonium sulfate precipitation and DE-52 anion-exchange column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E138A
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inactive, selenomethionine-substituted
E138Q
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inactive
R115A
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inactive
E138Q
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inactive
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R115A
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inactive
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E145A
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the mutant enzyme is defect in the deaminase reaction