Thymidylate kinase: Difference between revisions

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{{STRUCTURE_1e99|  PDB=1e99 | SIZE=350| SCENE= |right|CAPTION=Human thymidylate kinase complex with HIV prodrug AZTP, ADP (stick model) and Mg+2 ion (green) [[1e99]] }}
<StructureSection load='1e99' size='350' side='right' scene='' caption='Human thymidylate kinase complex with HIV prodrug AZTP, ADP (stick model) and Mg+2 ion (green)'>
 
== Function ==
== Function ==
'''Thymidylate kinase''' (TMK) catalyzes the conversion of thymidine-5’-phosphate (dTMP) and ATP to thymidine-5’-diphosphate and ADP.  TMK is important for DNA synthesis<ref>PMID:23394555</ref>.  Inhibitors of TMK include bisubstrate compounds of the type TP(n)X where P(n) are the number of phosphoryl groups and X is the nucleoside moiety of the acceptor.  For more details see [[Student Project 8 for UMass Chemistry 423 Spring 2015]].
'''Thymidylate kinase''' (TMK) catalyzes the conversion of thymidine-5’-phosphate (dTMP) and ATP to thymidine-5’-diphosphate and ADP.  TMK is important for DNA synthesis<ref>PMID:23394555</ref>.  Inhibitors of TMK include bisubstrate compounds of the type TP(n)X where P(n) are the number of phosphoryl groups and X is the nucleoside moiety of the acceptor.  For more details see [[Student Project 8 for UMass Chemistry 423 Spring 2015]].
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== Structural highlights ==
== Structural highlights ==
The active site of TMK contains HIV prodrug azido-thymidine, ADP and Mg+2 ion<ref>PMID:11071809</ref>.
The active site of TMK contains HIV prodrug azido-thymidine, ADP and Mg+2 ion<ref>PMID:11071809</ref>.
 
</StructureSection>
== 3D Structures of thymidylate kinase ==
== 3D Structures of thymidylate kinase ==


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Michal Harel, Alexander Berchansky, Joel L. Sussman