Nucleoside-phosphate kinase
| nucleoside phosphate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In
- ATP + nucleoside phosphate ADP + nucleoside diphosphate
Thus, the two
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor.[4] The systematic name of this enzyme class is ATP:nucleoside-phosphate phosphotransferase. This enzyme is also called NMP-kinase, or nucleoside-monophosphate kinase.
Structure
A number of
The [P-loop] typically has the amino acid sequence of Gly-X-X-X-X-Gly-Lys.[6] Similar sequences are found in many other nucleotide-binding proteins.
Mechanism
Metal ion interaction
To allow for interaction with this class of enzymes,
The metal ion interaction facilitates binding by holding the ATP molecule in a position allowing for specific binding to the active site and by providing additional points for binding between the substrate and the enzyme. This increases the binding energy.
Conformational changes
Binding of
The necessity of these conformational changes prevents the wasteful hydrolysis of ATP.
This enzyme mechanism is an example of
Biological function
Similar catalytic domains are present in a variety of proteins, including:
- ATP synthase
- Myosin, and other molecular motor proteins
- G protein and other proteins involved in signal transduction
- Helicases for unwinding DNA and RNA
- Pyrimidine metabolism
Evolution
When a phylogenetic tree composed of members of the nucleoside-phosphate kinase family was made,[14] it showed that these enzymes had originally diverged from a common ancestor into long and short varieties. This first change was drastic – the three-dimensional structure of the lid domain changed significantly.
Following the evolution of long and short varieties of NMP-kinases, smaller changes in the amino acid sequences resulted in the differentiation of subcellular localization.
References
- ^ Boyer PD, Lardy H, Myrback K, eds. (1962). The Enzymes. Vol. 6 (2nd ed.). New York: Academic Press. pp. 139–149.
- PMID 13363863.
- PMID 14392176.
- PMID 14401179.
- S2CID 11786335.
- PMID 7880812.
- PMID 8805521.
- ISBN 0-7167-3051-0. Retrieved 2016-01-08.
- S2CID 20874015.
- PMID 198550.
- PMID 1548697.
- PMID 8594191.
- PMID 7663945.
- S2CID 24934783.
