Bifunctional purine biosynthesis protein PURH
From Proteopedia
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== Function == | == Function == | ||
| - | aminoimidazole 4-carboxamide-4-carboxylic acid (AICAR) | + | Bifunctional purine biosynthesis protein PURH (PURH) is a bifunctional enzyme which catalyzes the last two steps in purine biosynthesis. PURH is composed of 2 functionally independent domains linked by a flexible domain. The N-terminal domain possesses IMP cyclohydrolase activity and the C-terminal domain possesses aminoimidazole 4-carboxamide ribonucleotide transformylase activity<ref>PMID:22139174</ref>. |
| + | aminoimidazole 4-carboxamide-4-carboxylic acid (AICAR) is an allosteric activator of AMP-activated protein kinase. | ||
== Disease == | == Disease == | ||
Revision as of 09:50, 22 April 2020
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3D structures of bifunctional purine biosynthesis protein PURH
Updated on 22-April-2020
1pkx - hPURH + XMP - human
5uy8, 5uz0 - hPURH + AICAR + inhibitor
1p4r, 1pl0 - hPURH + AICAR + XMP + inhibitor
1oz0 - cPURH - chicken
1thz, 2iu3, 2iu0, 2b1g, 2b1i - cPURH + inhibitor
1m9n - cPURH + AICAR + XMP
1zcz - PURH - Thermotoga maritima
3zzm - MtPURH + CFAIR - Mycobacterium tuberculosis
4a1o - MtPURH + AICAR + CFAIR
2ntm - MetPURH - Methanothermobacter thermautotrophicus
2ntl - MetPURH + AICAR
2ntk - MetPURH + IMP
References
- ↑ Qiu X, Yuan Y, Gao Y. Expression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Dec 1;67(Pt 12):1590-4., doi: 10.1107/S1744309111039960. Epub 2011 Nov 26. PMID:22139174 doi:http://dx.doi.org/10.1107/S1744309111039960
