Literature summary for 3.5.4.13 extracted from

Johansson, E.; Fan?, M.; Bynck, J.H.; Neuhard, J.; Larsen, S.; Sigurskjold, B.W.; Christensen, U.; Willemoes, M.
Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes (2005), J. Biol. Chem., 280, 3051-3059.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
wild-type and mutant E138A, in complex with Mg2+ and dUTP, and dCTP	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
E138A	no enzymic activity, no change in overall structure compared to wild-type	Escherichia coli
E138Q	no enzymic activity, no change in overall structure compared to wild-type	Escherichia coli
R115A	no enzymic activity, no change in overall structure compared to wild-type	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P28248	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
dCTP + H2O = dUTP + NH3	reaction involves S111, A124, E138 and two water molecules	Escherichia coli	a

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Release 2023.1 (January 2023)