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Information on EC 3.5.4.30 - dCTP deaminase (dUMP-forming) and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57872

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IUBMB Comments
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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Methanocaldococcus jannaschii
UNIPROT: Q57872
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The enzyme appears in selected viruses and cellular organisms
Synonyms
mj0430, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dCTP deaminase-dUTPase
DCD-DUT
-
-
-
-
dCTP deaminase-dUTP pyrophosphatase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of amidines
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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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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
?
-
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
dCTP + H2O
dUMP + diphosphate + NH3
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
dependent on, optimal concentration: 2-5 mM
NaCl
maximum activity at 0.15 or 2 M
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha,beta-imido-dUTP
-
dUTP
80% inhibition at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17.6
dCTP
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
50% activity at pH 6 and pH 9
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the bifunctional dCTP deaminase-dUTPase coordinates the deamination and triphosphate cleavage reactions
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
77900
enzyme with addition of six histidines at the N-terminus, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
two trimers can assemble into a hexamer by stacking on top of each other
homotrimer
the subunits are composed of a central distorted beta.barrel surrounded by two beta-sheets and four helices
trimer
two trimers can assemble into a hexamer by stacking on top of each other
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo form complexed with dCTP and dUTP, hanging drop vapor diffusion method
hanging drop vapor diffusion technique, the crystal structure is determined to 1.88 A resolution
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E145A
the mutant enzyme is defect in the deaminase reaction
E145Q
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
thermostable, loss of 30% activity after 10 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, H.; Xu, H.; Graham, D.E.; White, R.H.
The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase
J. Biol. Chem.
278
11100-11106
2003
Methanocaldococcus jannaschii (Q57872), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Huffman, J.L.; Li, H.; White, R.H.; Tainer, J.A.
Structural basis for recognition and catalysis by the bifunctional dCTP deaminase and dUTPase from Methanococcus jannaschii
J. Mol. Biol.
331
885-896
2003
Methanocaldococcus jannaschii (Q57872)
Manually annotated by BRENDA team
Siggaard, J.H.; Johansson, E.; Vognsen, T.; Helt, S.S.; Harris, P.; Larsen, S.; Willemoes, M.
Concerted bifunctionality of the dCTP deaminase-dUTPase from Methanocaldococcus jannaschii: a structural and pre-steady state kinetic analysis
Arch. Biochem. Biophys.
490
42-49
2009
Methanocaldococcus jannaschii (Q57872)
Manually annotated by BRENDA team
Johansson, E.; Bjornberg, O.; Nyman, P.O.; Larsen, S.
Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases
J. Biol. Chem.
278
27916-27922
2003
Methanocaldococcus jannaschii (Q57872), Methanocaldococcus jannaschii DSM 2661 (Q57872)
Manually annotated by BRENDA team