Literature summary for 3.5.4.12 extracted from

Hou, H.F.; Liang, Y.H.; Li, L.F.; Su, X.D.; Dong, Y.H.
Crystal structures of Streptococcus mutans 2-deoxycytidylate deaminase and its complex with substrate analog and allosteric regulator dCTP x Mg2+ (2008), J. Mol. Biol., 377, 220-231.

Search for more literature for 3.5.4.12

Activating Compound

Activating Compound	Comment	Organism	Structure
dCTP	an allosteric activator, in complex with Mg2+	Streptococcus mutans

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)	Streptococcus mutans

Crystallization (Commentary)

Crystallization (Comment)	Organism
dCMP deaminase in complex with dCTP and an intermediate analogue, X-ray diffraction structure determination and analysis at 1.66-3.0 A resolution, the crystal structure of the free-state enzyme is determined by the zinc multiwavelength anomalous dispersion, MAD, method	Streptococcus mutans

Inhibitors

Inhibitors	Comment	Organism	Structure
dTTP	an allosteric inhibitor	Streptococcus mutans

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	can partially substitute for Mg2+, 50% of the activity with Mg2+	Streptococcus mutans
Mg2+	required for activity, in complex with activator dCTP, can be substituted by Ca2+ or Mn2+, but not by Zn2+, Co2+, Ni2+, and Cu2+	Streptococcus mutans
Mn2+	can partially substitute for Mg2+, 26% of the activity with Mg2+	Streptococcus mutans
additional information	Co2+, Ni2+, and Cu2+ cannot substitute for Mg2+	Streptococcus mutans
Zn2+	two conserved motifs are involved in the binding of Zn2+, Zn2+ cannot substitute for Mg2+	Streptococcus mutans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
dCMP + H2O	Streptococcus mutans	the regulation signal is transmitted by Arg4 from the allosteric site to the active site via modifications in the interactions at the interface where the substrate binding pocket is involved and the relocations of Arg26, His65, Tyr120, and Arg121 to envelope the active site in order to stabilize substrate binding in the complex, allosteric mechanism for enzyme regulation, regulator binding structure, overview	dUMP + NH3	-	?

Organism

Organism	UniProt	Comment	Textmining
Streptococcus mutans	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration	Streptococcus mutans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
dCMP + H2O	the regulation signal is transmitted by Arg4 from the allosteric site to the active site via modifications in the interactions at the interface where the substrate binding pocket is involved and the relocations of Arg26, His65, Tyr120, and Arg121 to envelope the active site in order to stabilize substrate binding in the complex, allosteric mechanism for enzyme regulation, regulator binding structure, overview	Streptococcus mutans	dUMP + NH3	-	?
dCMP + H2O	a conserved motif, G43YNG46, is involved in the binding of dCTP, N-terminal Arg4, a key residue located between two monomers, binds strongly to the gamma phosphate group of dCTP, active site structure and substrate binding, overview	Streptococcus mutans	dUMP + NH3	-	?

Subunits

Subunits	Comment	Organism
hexamer	homohexamer, subunits adopt a three-layer alpha/beta/alpha sandwich fold	Streptococcus mutans
More	monomeric and quarternary structure analysis, overview	Streptococcus mutans

Synonyms

Synonyms	Comment	Organism
2-deoxycytidylate deaminase	-	Streptococcus mutans
deoxycytidine-5'-monophosphate deaminase	-	Streptococcus mutans

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Streptococcus mutans

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Streptococcus mutans

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Release 2023.1 (January 2023)