Difference between revisions of "Kinase Group NDK"
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The human RP2 gene has relatively weak similarity to the NDK domain, and is counted a member of the family. It fails to show kinase activity in vitro, and has altered the catalytic histidine to a phenylalanine, making this a [[pseudokinases|pseudokinase]] <cite>Yoon</cite>. | The human RP2 gene has relatively weak similarity to the NDK domain, and is counted a member of the family. It fails to show kinase activity in vitro, and has altered the catalytic histidine to a phenylalanine, making this a [[pseudokinases|pseudokinase]] <cite>Yoon</cite>. | ||
| − | + | The NDK family has the following subfamilies: | |
| − | + | ||
| − | [[ | + | ====[[Kinase_Subfamily_NDKA|NDKA]]==== |
| + | Includes several with protein kinase activity | ||
| − | [[ | + | ====[[Kinase_Subfamily_NDKB|NDKB]]==== |
| − | [[ | + | ====[[Kinase_Subfamily_NDKC|NDKC]]==== |
| − | [[Kinase_Subfamily_NDKE|NDKE]] | + | ====[[Kinase_Subfamily_NDKD|NDKD]]==== |
| + | Dual domain kinases involved in microtubule and cilia function | ||
| + | |||
| + | ====[[Kinase_Subfamily_NDKE|NDKE]]==== | ||
| + | Thioredoxin-NDK fusions also implicated in cilium biology. | ||
=== References === | === References === | ||
Revision as of 15:29, 9 February 2022
Kinase Classification: Group NDK
Nucleoside Diphosphate Kinases (NDK or NDPK) use ATP to transfer a phosphate to other nucleoside diphosphates, using a phospho-histidine intermediate. One of 9 human NDKs was shown to have protein kinase activity, and protein kinase activity was also reported for members in Drosophila, Neurospora, Paramecium and pea.
This family is universal in eukaryotes, and best known to phosphorylate nucleoside diphosphates to nucleoside triphosphates. NDKs have a ferridoxin-like fold, and use a phospho-histidine intermediate during catalysis (the donor phosphate is transiently attached to a His residue on the NDK).
Four of the 10 human NDKs belong to the NDKA subfamily which has been shown to have protein histidine kinase activity in many species, including animals, fungi and a plant.
In prokaryotes, autophosphorylation of NDKs on both histidine and serine has been reported for E. coli [1] and Myxococcus xanthus [2].
The human RP2 gene has relatively weak similarity to the NDK domain, and is counted a member of the family. It fails to show kinase activity in vitro, and has altered the catalytic histidine to a phenylalanine, making this a pseudokinase [3].
The NDK family has the following subfamilies:
NDKA
Includes several with protein kinase activity
NDKB
NDKC
NDKD
Dual domain kinases involved in microtubule and cilia function
NDKE
Thioredoxin-NDK fusions also implicated in cilium biology.
References
- Almaula N, Lu Q, Delgado J, Belkin S, and Inouye M. Nucleoside diphosphate kinase from Escherichia coli. J Bacteriol. 1995 May;177(9):2524-9. DOI:10.1128/jb.177.9.2524-2529.1995 |
- Yoon JH, Qiu J, Cai S, Chen Y, Cheetham ME, Shen B, and Pfeifer GP. The retinitis pigmentosa-mutated RP2 protein exhibits exonuclease activity and translocates to the nucleus in response to DNA damage. Exp Cell Res. 2006 May 1;312(8):1323-34. DOI:10.1016/j.yexcr.2005.12.026 |
