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| | {{STRUCTURE_2jbm| PDB=2jbm | SCENE= }} | | {{STRUCTURE_2jbm| PDB=2jbm | SCENE= }} |
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| - | '''QPRTASE STRUCTURE FROM HUMAN'''
| + | ===QPRTASE STRUCTURE FROM HUMAN=== |
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| - | ==Overview==
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| - | Human quinolinate phosphoribosyltransferase (EC 2.4.2.19) (hQPRTase) is a member of the type II phosphoribosyltransferase family involved in the catabolism of quinolinic acid (QA). It catalyses the formation of nicotinic acid mononucleotide from quinolinic acid, which involves a phosphoribosyl transfer reaction followed by decarboxylation. hQPRTase has been implicated in a number of neurological conditions and in order to study it further, we have carried out structural and kinetic studies on recombinant hQPRTase. The structure of the fully active enzyme overexpressed in Escherichia coli was solved using multiwavelength methods to a resolution of 2.0 A. hQPRTase has a alpha/beta barrel fold sharing a similar overall structure with the bacterial QPRTases. The active site of hQPRTase is located at an alpha/beta open sandwich structure that serves as a cup for the alpha/beta barrel of the adjacent subunit with a QA binding site consisting of three arginine residues (R102, R138 and R161) and two lysine residues (K139 and K171). Mutation of these residues affected substrate binding or abolished the enzymatic activity. The kinetics of the human enzyme are different to the bacterial enzymes studied, hQPRTase is inhibited competitively and non-competitively by one of its substrates, 5-phosphoribosylpyrophosphate (PRPP). The human enzyme adopts a hexameric arrangement, which places the active sites in close proximity to each other.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17868694}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17868694 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17868694}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pyridine nucleotide biosynthesis]] | | [[Category: Pyridine nucleotide biosynthesis]] |
| | [[Category: Transferase]] | | [[Category: Transferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:39:09 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:05:14 2008'' |
Revision as of 01:05, 29 July 2008
Template:STRUCTURE 2jbm
QPRTASE STRUCTURE FROM HUMAN
Template:ABSTRACT PUBMED 17868694
About this Structure
2JBM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and kinetic characterization of quinolinate phosphoribosyltransferase (hQPRTase) from homo sapiens., Liu H, Woznica K, Catton G, Crawford A, Botting N, Naismith JH, J Mol Biol. 2007 Oct 26;373(3):755-63. Epub 2007 Aug 24. PMID:17868694
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