This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Pantothenate kinase
From Proteopedia
| Line 10: | Line 10: | ||
== Disease == | == Disease == | ||
Mutations in PanK II cause the autosomal-recessive disorder Pantothenate kinase-associated neurodegeneration<ref>PMID:15911822</ref>. | Mutations in PanK II cause the autosomal-recessive disorder Pantothenate kinase-associated neurodegeneration<ref>PMID:15911822</ref>. | ||
| + | |||
| + | == Structural highlights == | ||
| + | Pantothenate binds in a buried pocket at the PanK dimer interface<ref>PMID:16905099</ref>. | ||
==3D structures of pantothenate kinase== | ==3D structures of pantothenate kinase== | ||
Revision as of 07:50, 14 June 2016
Contents |
Function
Pantothenate kinase (PanK) phosphorylates pantothenate (vitamin B5) (PAU) to form 4’-phosphopantothenate (PPT) using ATP as phosphate source. This is the first step in coenzyme A biosynthesis[1].
Three types of PanK are known.
- PanK I found in bacteria
- PanK II found mostly in eukaryotes
- PanK III found in bacteria and known as CoaX.
Disease
Mutations in PanK II cause the autosomal-recessive disorder Pantothenate kinase-associated neurodegeneration[2].
Structural highlights
Pantothenate binds in a buried pocket at the PanK dimer interface[3].
3D structures of pantothenate kinase
Updated on 14-June-2016
References
- ↑ . PanK is regulated by feedback inhibition by CoA and its thioesters.PMID:9890959
- ↑ Pellecchia MT, Valente EM, Cif L, Salvi S, Albanese A, Scarano V, Bonuccelli U, Bentivoglio AR, D'Amico A, Marelli C, Di Giorgio A, Coubes P, Barone P, Dallapiccola B. The diverse phenotype and genotype of pantothenate kinase-associated neurodegeneration. Neurology. 2005 May 24;64(10):1810-2. PMID:15911822 doi:http://dx.doi.org/10.1212/01.WNL.0000161843.52641.EC
- ↑ Hong BS, Yun MK, Zhang YM, Chohnan S, Rock CO, White SW, Jackowski S, Park HW, Leonardi R. Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties. Structure. 2006 Aug;14(8):1251-61. PMID:16905099 doi:10.1016/j.str.2006.06.008
