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Literature summary for 2.7.4.9 extracted from

  • Biswas, A.; Jasti, S.; Jeyakanthan, J.; Sekar, K.
    Role of sequence evolution and conformational dynamics in the substrate specificity and oligomerization mode of thymidylate kinases (2017), J. Biomol. Struct. Dyn., 35, 2136-2154 .
    View publication on PubMed
Search for more literature for 2.7.4.9

Cloned(Commentary)

Cloned (Comment) Organism
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 Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii Q970Q8
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Sulfurisphaera tokodaii DSM 16993 Q970Q8
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Purification (Commentary)

Purification (Comment) Organism
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 Sulfurisphaera tokodaii

Subunits

Subunits Comment Organism
homodimer
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 Sulfurisphaera tokodaii

Synonyms

Synonyms Comment Organism
thymidylate kinase
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 Sulfurisphaera tokodaii
TMK
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 Sulfurisphaera tokodaii

General Information

General Information Comment Organism
drug target thymidylate kinase is a key enzyme for the synthesis of DNA, making it an important target for the development of anticancer, antibacterial and antiparasitic drugs Sulfurisphaera tokodaii
evolution study on influence of sequence evolution and conformational dynamics on its quaternary structure and function. Based on extensive sequence and structure analyses, the study detects several non-conserved residues which are linked by co-evolution and are implicated in the observed variations in flexibility, oligomeric assembly and substrate specificity among the homologs. These lead to differences in the pattern of interactions at the active site in thymidylate kinases of different specificity Sulfurisphaera tokodaii
physiological function key enzyme for the synthesis of DNA Sulfurisphaera tokodaii