2.7.4.9: dTMP kinase
This is an abbreviated version!
For detailed information about dTMP kinase, go to the full flat file.
Reaction
Synonyms
ATP: TMP phosphotransferase, Cdc8, deoxythymidine 5'-monophosphate kinase, deoxythymidine monophosphate kinase, dTMP kinase, dTMP kinases, dTMPK, human thymidine monophosphate kinase (hTMPK), kinase, thymidine monophosphate (phosphorylating), kinase, thymidylate (phosphorylating), ORF454, PfTMK, S. aureus thymidylate kinase, thymidine 5'-monophosphate kinase, thymidine kinase, thymidine monophosphate kinase, thymidylate kinase, thymidylate monophosphate kinase, thymidylic acid kinase, thymidylic kinase, TK1, TMK, TMP kinase, TMPK, TMPKmt, TTHA1607, TYMK
ECTree
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General Stability
General Stability on EC 2.7.4.9 - dTMP kinase
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dissociation of the native dimeric species of the enzyme occurs at an urea concentration of around 4 M, leading to the accumulation of partially folded monomers that unfold totally at urea concentrations above 5.5 M
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midpoint transition is 3.0 M urea for the wild-type enzyme and 3.3 M for the G146A mutant enzyme
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the canonical enzyme is stable and its activity is not affected by the presence of NaCl
the enzyme from outer mitochondrial membrane is unstable and loses activity rapidly, it also loses activity in the presence of a high concentration of NaCl
the enzyme is very labile and can be stabilized for long periods of time by its substrate thymidine 5'-monophosphate in the presence of 2-mercaptoethanol
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the enzyme is very unstable and may be stabilized in the presence of 2-mercaptoethanol with dTMP, dTDP, or ADP but not with ATP, MgATP2- or mercaptoethanol alone
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the stability of the enzyme is maintained during purification by the constant presence of dTMP and 2-mercaptoethanol and by the elimination of substrate-destoying phosphatase activity
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