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Literature summary for 2.7.4.9 extracted from

  • Fioravanti, E.; Adam, V.; Munier-Lehmann, H.; Bourgeois, D.
    The crystal structure of Mycobacterium tuberculosis thymidylate kinase in complex with 3'-azidodeoxythymidine monophosphate suggests a mechanism for competitive inhibition (2005), Biochemistry, 44, 130-137.
    View publication on PubMed

Application

Application Comment Organism
drug development potential target for the development of antituberculosis drugs Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
cocrystals with 3’-azido-3’-deoxythymidine 5'-monophosphate and deoxythymidine Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
3'-azido-3'-deoxythymidine
-
Mycobacterium tuberculosis
3'-azido-3'-deoxythymidine 5'-monophosphate
-
Mycobacterium tuberculosis
deoxythymidine
-
Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ bound to enzyme, displacement of Mg2+ is responsible for inhibitory effect of 3’-azido-3’-deoxythymidine 5'-monophosphate Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + dTMP Mycobacterium tuberculosis involved in dTTP metabolism, essential for cell proliferation ADP + dTDP
-
r

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WKE1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + dTMP
-
Mycobacterium tuberculosis ADP + dTDP
-
r
ATP + dTMP involved in dTTP metabolism, essential for cell proliferation Mycobacterium tuberculosis ADP + dTDP
-
r

Subunits

Subunits Comment Organism
dimer crystal structure analysis Mycobacterium tuberculosis