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Literature summary for 2.7.4.9 extracted from
- The structure of thymidylate kinase from Candida albicans reveals a unique structural element (2017), Biochemistry, 56, 4360-4370 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Candida albicans |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| sitting drop vapour diffusion method, the structure of thymidylate kinase from Candida albicans, determined by X-ray crystallography, 2.45 A resolution | Candida albicans |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00107 | - |
dGMP | pH 7.4, temperature not specified in the publication, NADH coupled assay | Candida albicans |  |
| 0.0045 | - |
3'-azido-3'-deoxythymidine monophosphate | pH 7.4, temperature not specified in the publication, NADH coupled assay | Candida albicans | |
| 0.0062 | - |
TMP | pH 7.4, temperature not specified in the publication, NADH coupled assay | Candida albicans | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Candida albicans | Q59TV7 | - |
- |
| Candida albicans ATCC MYA-2876 | Q59TV7 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Candida albicans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 3'-azido-3'-deoxythymidine monophosphate | - |
Candida albicans | ADP + 3'-azido-3'-deoxythymidine diphosphate | - |
? | |
| ATP + 3'-azido-3'-deoxythymidine monophosphate | - |
Candida albicans ATCC MYA-2876 | ADP + 3'-azido-3'-deoxythymidine diphosphate | - |
? | |
| ATP + dGMP | - |
Candida albicans | ADP + dGDP | - |
? | |
| ATP + dGMP | - |
Candida albicans ATCC MYA-2876 | ADP + dGDP | - |
? | |
| ATP + TMP | - |
Candida albicans | ADP + TDP | - |
? | |
| ATP + TMP | - |
Candida albicans ATCC MYA-2876 | ADP + TDP | - |
? | |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.006 | - |
dGMP | pH 7.4, temperature not specified in the publication, NMR assay | Candida albicans | |
| 0.008 | - |
dGMP | pH 7.4, temperature not specified in the publication, NADH coupled assay | Candida albicans | |
| 0.3 | - |
3'-azido-3'-deoxythymidine monophosphate | pH 7.4, temperature not specified in the publication, NADH coupled assay | Candida albicans | |
| 0.5 | - |
3'-azido-3'-deoxythymidine monophosphate | pH 7.4, temperature not specified in the publication, NMR assay | Candida albicans | |
| 6.9 | - |
TMP | pH 7.4, temperature not specified in the publication, NADH coupled assay | Candida albicans | |
| 8.7 | - |
TMP | pH 7.4, temperature not specified in the publication, NMR assay | Candida albicans | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| drug target | the enzyme is a potential drug target for antifungal drug discovery for a number of reasons. First, it shows several structural differences compared to its human counterpart. These include the Ca-loop, as well as significant shifts in the location of helices and strands. The structural differences can form potential binding sites for allosteric inhibitors. Second, the fact the CaTMPK can utilize dGMP as a substrate suggests that competitive inhibitors that resemble purine nucleosides may preferentially bind to CaTMPK versus the human enzyme | Candida albicans |
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