deletion mutant 65-79, invisible 241-245
mutant C9S, C45S, C59S, C146S, invisible 167-168
mutant C9S, C45S, C59S, C146S, invisible 63-76
mutant C9S, C45S, C59S, C146S, E247A, invisible 62-79, 117
mutant C9S, C45S, C59S, C146S, invisible 64-76
mutant C9S, C45S, C59S, C146S, invisible 65-76
mutant C9S, C45S, C59S, C146S, invisible 61-70, 168
mutant C9S, C45S, C59S, C146S, invisible 61-74, 167
mutant C9S, C45S, C59S, C146S, invisible 59-76, 168
mutant C9S, C45S, C59S, C146S, invisible 62-69
mutant C9S, C45S, C59S, C146S, invisible 63-70
mutant C9S, C45S, C59S, C146S, invisible 64-69
Structural basis for substrate specificities of cellular deoxyribonucleoside kinases. Nat Struct Biol.
Kinetic analysis of human deoxycytidine kinase with the true phosphate donor uridine triphosphate.
Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate.
Structure and function of cellular deoxyribonucleoside kinases
Structure of human dCK suggests strategies to improve anticancer and antiviral therapy.
The structure of human deoxycytidine kinase in complex with clofarabine reveals key interactions for prodrug activation.
Structural basis for the preference of UTP over ATP in human deoxycytidine kinase: illuminating the role of main-chain reorganization.
Structures of human deoxycytidine kinase product complexes.
Nonenantioselectivity property of human deoxycytidine kinase explained by structures of the enzyme in complex with L- and D-nucleosides.
Structural basis for activation of the therapeutic L-nucleoside analogs 3TC and troxacitabine by human deoxycytidine kinase.
Elucidation of different binding modes of purine nucleosides to human deoxycytidine kinase.
Structural basis for substrate promiscuity of dCK.
Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase.
Lead optimization and structure-based design of potent and bioavailable deoxycytidine kinase inhibitors.
Structural and kinetic characterization of human deoxycytidine kinase variants able to phosphorylate 5-substituted deoxycytidine and thymidine analogues .
The sugar ring of the nucleoside is required for productive substrate positioning in the active site of human deoxycytidine kinase (dCK): implications for the development of dCK-activated acyclic guanine analogues.
Post-translational phosphorylation of serine 74 of human deoxycytidine kinase favors the enzyme adopting the open conformation making it competent for nucleoside binding and release.
This enzyme is a non-enantioselective enzyme, which can phosphorylate both L- and D-enantiomers of nuceloside. Moreover, this enzyme constitute a family of three related non-enantioselective enzymes, along with thymidine kinase (EC 2.7.1.21; UniProt;O00142) and deoxyguanosine kinase (EC 2.7.1.113; UniProt;Q16854). Moreover, this enzyme is also homologous to deoxynucleoside kinase (EC 2.7.1.145; S00672 in EzCatDB). This enzyme catalyzes transfer of phosphoryl group from NTP to 5'-hydroxyl group of deoxycytidine, as follows: (0) Arg128 may modulate the activity of Glu53. Magnesium ion, bound to Ser35 and Glu127, may stabilize the negative charge on the beta- and gamma-phosphate groups. (1) Glu53 acts as a general base to deprotonate and activate 5'-hydroxyl group of the substrate, deoxycytidine. (2) The activated 5'-hydroxyl oxygen makes a nucleophilic attack on the gamma-phosphate group of NTP. (SN2-like reaction) (3) During the transition state, Arg128, Arg192 and Arg194 may stabilize the transferrd group, the gamma-phosphate, whereas the sidechain of Lys34 and Arg192 might stabilize the leaving group, beta- and alpha-phosphate groups, along with the mainchain of Ala32, Gly33, and Lys34. At the same time, the magnesium ion might stabilize the negative charge on the transferred group, the gamma-phosphate, and the leaving group, the beta-phosphate group.