BRENDA - Enzyme Database
show all sequences of 2.1.2.8

Evidence from 18O feeding studies for hydroxyl group donor in the reaction catalyzed by cytidylate hydroxymethylase MilA

Chen, C.; Gao, T.; Zhao, G.; Deng, Z.; Hu, S.; Xu, H.; He, X.; Chin. Sci. Bull. 58, 864-868 (2013)
No PubMed abstract available

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
T4virus
the hydroxymethylation is catalyzed by dCMP hydroxymethylase, which transfers a methylene group from methylenetetrahydrofolate to C5 of dCMP and then uses a water molecule to hydrate the methylene group to form hydroxymethyl-dCMP, one precursor for phage DNA replication
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
T4virus
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
the hydroxymethylation is catalyzed by dCMP hydroxymethylase, which transfers a methylene group from methylenetetrahydrofolate to C5 of dCMP and then uses a water molecule to hydrate the methylene group to form hydroxymethyl-dCMP, one precursor for phage DNA replication
735967
T4virus
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
-
-
-
?
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
the enzyme uses the solvent water as the hydroxyl group donor
735967
T4virus
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
-
-
-
?
additional information
5-hydroxymethylcytosine in phage is formed by hydroxymethylation of the cytosine base in deoxycytidylate (dCMP) by deoxycytidylate hydroxymethylase, which uses the solvent water as the hydroxyl group donor
735967
T4virus
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
5,10-methylenetetrahydrofolate
-
T4virus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
5,10-methylenetetrahydrofolate
-
T4virus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
T4virus
the hydroxymethylation is catalyzed by dCMP hydroxymethylase, which transfers a methylene group from methylenetetrahydrofolate to C5 of dCMP and then uses a water molecule to hydrate the methylene group to form hydroxymethyl-dCMP, one precursor for phage DNA replication
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
the hydroxymethylation is catalyzed by dCMP hydroxymethylase, which transfers a methylene group from methylenetetrahydrofolate to C5 of dCMP and then uses a water molecule to hydrate the methylene group to form hydroxymethyl-dCMP, one precursor for phage DNA replication
735967
T4virus
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
-
-
-
?
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
the enzyme uses the solvent water as the hydroxyl group donor
735967
T4virus
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
-
-
-
?
additional information
5-hydroxymethylcytosine in phage is formed by hydroxymethylation of the cytosine base in deoxycytidylate (dCMP) by deoxycytidylate hydroxymethylase, which uses the solvent water as the hydroxyl group donor
735967
T4virus
?
-
-
-
-
Other publictions for EC 2.1.2.8
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
735967
Chen
-
Evidence from 18O feeding stud ...
T4virus
Chin. Sci. Bull.
58
864-868
2013
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659367
Shen
Escherichia coli nucleoside di ...
Escherichia coli
J. Biol. Chem.
279
32225-32232
2004
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485792
Song
Crystal structure of deoxycyti ...
Escherichia virus T4
EMBO J.
18
1104-1113
1999
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1
1
1
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485791
Hardy
Electrostatic guidance of cata ...
Escherichia virus T4
Biochemistry
34
8422-8432
1995
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2
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485789
Graves
Kinetic and equilibrium alpha- ...
Escherichia virus T4
Biochemistry
33
13049-13056
1994
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3
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485790
Butler
Evidence from 18O exchange stu ...
Escherichia virus T4
Biochemistry
33
10521-10526
1994
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1
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2
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4
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485788
Mathews
Enzyme interactions involving ...
Escherichia virus T4
Adv. Exp. Med. Biol.
338
563-570
1993
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485787
Subramaniam
On the inhibition of deoxycyti ...
Escherichia virus T4
Arch. Biochem. Biophys.
275
11-15
1989
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485783
Lamm
Deoxycytidylate hydroxymethyla ...
Enterobacteria phage T2, Enterobacteria phage T6, Escherichia virus T4
Eur. J. Biochem.
172
553-563
1988
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485785
Lee
Deoxycytidylate hydroxymethyla ...
Escherichia virus T4
Biochemistry
27
1367-1373
1988
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485782
Lamm
Nucleotide sequence of the deo ...
Escherichia virus T4
Nucleic Acids Res.
15
3920
1987
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209854
Allen
T4 phage deoxyribonucleotide-s ...
Escherichia virus T4
J. Biol. Chem.
258
5746-5753
1983
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485786
North
T4 phage-coded deoxycytidylate ...
Escherichia virus T4
Biochem. Biophys. Res. Commun.
77
898-904
1977
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485780
Mathews
Virus-induced acquisition of m ...
bacteriophage T6r+
J. Biol. Chem.
239
2957-2963
1964
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485781
Pizer
Virus-induced acquisition of m ...
bacteriophage T6r+
J. Biol. Chem.
237
1251-1259
1962
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