Pyridoxal kinase
From Proteopedia
(Difference between revisions)
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- | {{STRUCTURE_2ddw| PDB=2ddw | SIZE=350| SCENE= |right|CAPTION=E. Coli pyridoxal kinase complex with pyridoxal [[2ddw]] }} | + | {{STRUCTURE_2ddw| PDB=2ddw | SIZE=350| SCENE= |right|CAPTION=E. Coli pyridoxal kinase 1 complex with pyridoxal [[2ddw]] }} |
+ | == Function == | ||
+ | '''Pyridoxal kinase''' (PDX) catalyzes the transfer of phosphate (Pi) from ATP to 5’ alcohol of pyridoxine, pyridoxamine and pyridoxal<ref>PMID:25655354</ref>. | ||
- | + | == Structural highlights == | |
+ | |||
+ | PDX1 active site<ref>PMID:16740960</ref>. | ||
== 3D Structures of pyridoxal kinase == | == 3D Structures of pyridoxal kinase == | ||
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*'''Pyridoxal kinase''' | *'''Pyridoxal kinase''' | ||
- | **[[1lhp]] – | + | **[[1lhp]] – sPDX – sheep<br /> |
- | **[[2f7k]] – | + | **[[2f7k]] – hPDX - human<br /> |
- | **[[2ddm]] – | + | **[[2ddm]] – EcPDX – ''Escherichia coli''<br /> |
- | **[[3h74]] – | + | **[[3h74]] – LpPDX – ''Lactobacillus planarum'' <br /> |
- | **[[3zs7]] – | + | **[[3zs7]] – PDX – ''Trypanosoma brucei'' <br /> |
- | **[[4c5j]] – | + | **[[4c5j]] – SaPDX – ''Staphylococcus aureus'' <br /> |
*Pyridoxal kinase complex with pyridoxal compounds | *Pyridoxal kinase complex with pyridoxal compounds | ||
- | **[[1rft]] – | + | **[[1rft]] – sPDX + Zn + K + AMPPCP + pyridoxamine<br /> |
- | **[[1rfu]] – | + | **[[1rfu]] – sPDX + Zn + ADP + pyridoxal-5’-phosphate<br /> |
- | **[[2ddw]] – | + | **[[2ddw]] – EcPDX + pyridoxal<br /> |
- | **[[4c5l]] – | + | **[[4c5l]] – SaPDX + pyridoxal<br /> |
- | **[[4c5n]] – | + | **[[4c5n]] – SaPDX + pyridoxal + AMPPCP<br /> |
- | **[[3fhx]] – | + | **[[3fhx]] – hPDX (mutant) + Mg + Na + ATP + pyridoxal + pyridoxal-5’-phosphate <br /> |
- | **[[3keu]] – | + | **[[3keu]] – hPDX + Mg + ATP + pyridoxal-5’-phosphate<br /> |
- | **[[4s1i]] – | + | **[[4s1i]] – EhPDX + Mg + pyridoxal-5’-phosphate - ''Entamoeba histolytica'' <br /> |
*Other pyridoxal kinase complexes | *Other pyridoxal kinase complexes | ||
- | **[[1lhr]] – | + | **[[1lhr]] – sPDX + Zn + K + ATP<br /> |
- | **[[1rfv]] – | + | **[[1rfv]] – sPDX + Zn + ADP <br /> |
- | **[[1ygj]], [[1ygk]], [[1yhj]] – | + | **[[1ygj]], [[1ygk]], [[1yhj]] – sPDX + roscovitine<br /> |
- | **[[2ajp]] – | + | **[[2ajp]] – hPDX + Mg + ANP <br /> |
- | **[[2ddo]] – | + | **[[2ddo]] – EcPDX1 + Mg + ATP + Pi<br /> |
- | **[[2i5b]] – | + | **[[2i5b]] – PDX + ADP – ''Bacillus subtilis''<br /> |
- | **[[2yxt]] – | + | **[[2yxt]] – hPDX + Na + Pi<br /> |
- | **[[2yxu]] – | + | **[[2yxu]] – hPDX + Mg + Na + ATP + Pi<br /> |
- | **[[3fhy]] – | + | **[[3fhy]] – hPDX (mutant) + Mg + Na + ATP <br /> |
- | **[[3hyo]] – | + | **[[3hyo]] – LpPDX + Mg + ADP <br /> |
- | **[[3ibq]] – | + | **[[3ibq]] – LpPDX + Mg + ATP <br /> |
- | **[[4en4]] – | + | **[[4en4]] – hPDX + Mg + ATP + ginkotoxin<br /> |
- | **[[4eoh]] – | + | **[[4eoh]] – hPDX + Na + theophylline<br /> |
- | **[[4c5k]] – | + | **[[4c5k]] – SaPDX + ADP<br /> |
- | **[[4c5m]] – | + | **[[4c5m]] – SaPDX + AMPPCP<br /> |
- | **[[4s1m]] – | + | **[[4s1m]] – EhPDX + Mg <br /> |
- | **[[4s1h]] – | + | **[[4s1h]] – EhPDX + Mg + ADP <br /> |
}} | }} |
Revision as of 09:12, 1 August 2016
Contents |
Function
Pyridoxal kinase (PDX) catalyzes the transfer of phosphate (Pi) from ATP to 5’ alcohol of pyridoxine, pyridoxamine and pyridoxal[1].
Structural highlights
PDX1 active site[2].
3D Structures of pyridoxal kinase
Updated on 01-August-2016
References
- ↑ di Salvo ML, Nogues I, Parroni A, Tramonti A, Milano T, Pascarella S, Contestabile R. On the mechanism of Escherichia coli pyridoxal kinase inhibition by pyridoxal and pyridoxal 5'-phosphate. Biochim Biophys Acta. 2015 Sep;1854(9):1160-6. doi: 10.1016/j.bbapap.2015.01.013., Epub 2015 Feb 3. PMID:25655354 doi:http://dx.doi.org/10.1016/j.bbapap.2015.01.013
- ↑ Safo MK, Musayev FN, di Salvo ML, Hunt S, Claude JB, Schirch V. Crystal structure of pyridoxal kinase from the Escherichia coli pdxK gene: implications for the classification of pyridoxal kinases. J Bacteriol. 2006 Jun;188(12):4542-52. PMID:16740960 doi:188/12/4542