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Literature summary for 2.7.4.6 extracted from

  • Kim, S.Y.; Song, E.J.; Chang, K.H.; Kim, E.; Chae, S.K.; Lee, H.; Lee, K.J.
    Oligomeric structures determine the biochemical characteristics of human nucleoside diphosphate kinases (2001), J. Biochem. Mol. Biol., 34, 355-364.
No PubMed abstract available

Protein Variants

Protein Variants Comment Organism
K135L isoform B, mutation in dimeric interface, defective DNA-binding and reduced stability of enzyme Homo sapiens
N69H isoform B, mutation in dimeric interface, defective DNA-binding and reduced stability of enzyme Homo sapiens
R34G isoform B, mutation in dimeric interface, defective DNA-binding and reduced stability of enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
isoforms A and B
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte isoforms A,B in the ratio 1:1 Homo sapiens
-
placenta isoforms A,B in the ratio 1:3 Homo sapiens
-

Subunits

Subunits Comment Organism
hexamer erythrocyte: different heterohexamers of isoforms A,B, main form is 3 * A + 3 * B, placenta: pure isoform B and heteromeric 1:1 mixture of isoforms A,B, SDS-PAGE Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
3 h, 50% loss of activity Homo sapiens