Literature summary for 2.7.1.74 extracted from

Sabini, E.; Hazra, S.; Konrad, M.; Lavie, A.
Nonenantioselectivity property of human deoxycytidine kinase explained by structures of the enzyme in complex with L- and D-nucleosides (2007), J. Med. Chem., 50, 3004-3014.

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant C9S/C45S/C59S/C146S in complex with D-2'-deoxycytidine and ADP, L-2'-deoxycytidine and ADP, and with 5-fluoro-1-(2R,5S)-[2-(hydroxymethyl)-1,3-oxathiolan-5-yl]cytosine, i.e. emtricitabine, and ADP. The ability of deoxycytidine kinase to phosphorylate the beta-form of enantiomeric nucleosides is due to both the nature of the enzymes active site and the nature of the substrates. Most of the binding interactions between substrate and enzyme are directed at the base moiety of the nucleoside	Homo sapiens

Crystallization (Comment)

Organism

mutant C9S/C45S/C59S/C146S in complex with D-2'-deoxycytidine and ADP, L-2'-deoxycytidine and ADP, and with 5-fluoro-1-(2R,5S)-[2-(hydroxymethyl)-1,3-oxathiolan-5-yl]cytosine, i.e. emtricitabine, and ADP. The ability of deoxycytidine kinase to phosphorylate the beta-form of enantiomeric nucleosides is due to both the nature of the enzymes active site and the nature of the substrates. Most of the binding interactions between substrate and enzyme are directed at the base moiety of the nucleoside

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C9S/C45S/C59S/C146S	mutation of the four surface-exposed Cys residues, constructued for crystallization. Mutant displays moderate kinetic differences in the catalytic efficiency when compared with wild-type	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P27707	-	-

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Release 2023.1 (January 2023)