BRENDA - Enzyme Database

Crystal structure of deoxycytidylate hydroxymethylase from bacteriophage T4, a component of the deoxyribonucleoside triphosphate-synthesizing complex

Song, H.K.; Sohn, S.H.; Suh, S.W.; EMBO J. 18, 1104-1113 (1999)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
2.1.2.8
gene 42 encoding enzyme is sequenced and expressed in Escherichia coli
Escherichia virus T4
Crystallization (Commentary)
EC Number
Crystallization
Organism
2.1.2.8
crystal structure in the presence of substrate dCMP at 1.6 A resolution
Escherichia virus T4
Engineering
EC Number
Amino acid exchange
Commentary
Organism
2.1.2.8
D179N
mutant with altered substrate preference, favoring dUMP rather than dCMP
Escherichia virus T4
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.1.2.8
28450
-
2 * 28450, homodimer of 246-residue subunits
Escherichia virus T4
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
Escherichia virus T4
-
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
enzyme forms part of phage DNA protection system
Escherichia virus T4
?
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
Escherichia virus T4
-
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
5-hydroxymethyl-dCMP is essential for DNA synthesis in phage T4
Escherichia virus T4
?
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
Escherichia virus T4
-
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
involved in biosynthesis of DNA precursor
Escherichia virus T4
?
2.1.2.8
additional information
Escherichia virus T4
enzyme functions in vivo as a component of a multienzyme complex called dNTP synthetase
?
-
-
-
2.1.2.8
additional information
Escherichia virus T4
enzyme is part of a complex efficiently channeling DNA precursors to the replication apparatus
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.1.2.8
Escherichia virus T4
P08773
-
-
Purification (Commentary)
EC Number
Commentary
Organism
2.1.2.8
purification of His6-tagged enzyme
Escherichia virus T4
Reaction
EC Number
Reaction
Commentary
Organism
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate = tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
catalytic mechanism
Escherichia virus T4
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
-
485792
Escherichia virus T4
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
enzyme forms part of phage DNA protection system
485792
Escherichia virus T4
?
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
-
485792
Escherichia virus T4
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
5-hydroxymethyl-dCMP is essential for DNA synthesis in phage T4
485792
Escherichia virus T4
?
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
-
485792
Escherichia virus T4
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
involved in biosynthesis of DNA precursor
485792
Escherichia virus T4
?
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
enzyme structure, dCMP binding site, folate cofactor binding site, way of substrate binding in the active site, key catalytic residue Cys-148 acts as nucleophile to attack the C6-atom of the cytosine base
485792
Escherichia virus T4
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
-
485792
Escherichia virus T4
?
2.1.2.8
additional information
enzyme functions in vivo as a component of a multienzyme complex called dNTP synthetase
485792
Escherichia virus T4
?
-
-
-
-
2.1.2.8
additional information
enzyme is part of a complex efficiently channeling DNA precursors to the replication apparatus
485792
Escherichia virus T4
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
2.1.2.8
homodimer
2 * 28450, homodimer of 246-residue subunits
Escherichia virus T4
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
2.1.2.8
5,10-methylenetetrahydrofolate
as cofactor; weak binding of the folate cofactor to enzyme
Escherichia virus T4
2.1.2.8
tetrahydrofolate
-
Escherichia virus T4
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
2.1.2.8
gene 42 encoding enzyme is sequenced and expressed in Escherichia coli
Escherichia virus T4
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
2.1.2.8
5,10-methylenetetrahydrofolate
as cofactor; weak binding of the folate cofactor to enzyme
Escherichia virus T4
2.1.2.8
tetrahydrofolate
-
Escherichia virus T4
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
2.1.2.8
crystal structure in the presence of substrate dCMP at 1.6 A resolution
Escherichia virus T4
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
2.1.2.8
D179N
mutant with altered substrate preference, favoring dUMP rather than dCMP
Escherichia virus T4
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.1.2.8
28450
-
2 * 28450, homodimer of 246-residue subunits
Escherichia virus T4
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
Escherichia virus T4
-
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
enzyme forms part of phage DNA protection system
Escherichia virus T4
?
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
Escherichia virus T4
-
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
5-hydroxymethyl-dCMP is essential for DNA synthesis in phage T4
Escherichia virus T4
?
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
Escherichia virus T4
-
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
involved in biosynthesis of DNA precursor
Escherichia virus T4
?
2.1.2.8
additional information
Escherichia virus T4
enzyme functions in vivo as a component of a multienzyme complex called dNTP synthetase
?
-
-
-
2.1.2.8
additional information
Escherichia virus T4
enzyme is part of a complex efficiently channeling DNA precursors to the replication apparatus
?
-
-
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.1.2.8
purification of His6-tagged enzyme
Escherichia virus T4
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
-
485792
Escherichia virus T4
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
enzyme forms part of phage DNA protection system
485792
Escherichia virus T4
?
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
-
485792
Escherichia virus T4
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
5-hydroxymethyl-dCMP is essential for DNA synthesis in phage T4
485792
Escherichia virus T4
?
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
-
485792
Escherichia virus T4
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
involved in biosynthesis of DNA precursor
485792
Escherichia virus T4
?
2.1.2.8
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate
enzyme structure, dCMP binding site, folate cofactor binding site, way of substrate binding in the active site, key catalytic residue Cys-148 acts as nucleophile to attack the C6-atom of the cytosine base
485792
Escherichia virus T4
tetrahydrofolate + 5-hydroxymethyldeoxycytidylate
-
485792
Escherichia virus T4
?
2.1.2.8
additional information
enzyme functions in vivo as a component of a multienzyme complex called dNTP synthetase
485792
Escherichia virus T4
?
-
-
-
-
2.1.2.8
additional information
enzyme is part of a complex efficiently channeling DNA precursors to the replication apparatus
485792
Escherichia virus T4
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
2.1.2.8
homodimer
2 * 28450, homodimer of 246-residue subunits
Escherichia virus T4