1b66: Difference between revisions

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[[Image:1b66.png|left|200px]]
{{STRUCTURE_1b66|  PDB=1b66  |  SCENE=  }}  
{{STRUCTURE_1b66|  PDB=1b66  |  SCENE=  }}  
===6-PYRUVOYL TETRAHYDROPTERIN SYNTHASE===
{{ABSTRACT_PUBMED_10024455}}


===6-PYRUVOYL TETRAHYDROPTERIN SYNTHASE===
==Disease==
[[http://www.uniprot.org/uniprot/PTPS_RAT PTPS_RAT]] Note=Deficiency leads to phenylketonuria.


{{ABSTRACT_PUBMED_10024455}}
==Function==
[[http://www.uniprot.org/uniprot/PTPS_RAT PTPS_RAT]] Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:010024455</ref><ref group="xtra">PMID:010737935</ref><references group="xtra"/>
<ref group="xtra">PMID:010024455</ref><ref group="xtra">PMID:010737935</ref><references group="xtra"/><references/>
[[Category: 6-pyruvoyltetrahydropterin synthase]]
[[Category: 6-pyruvoyltetrahydropterin synthase]]
[[Category: Rattus rattus]]
[[Category: Rattus rattus]]

Revision as of 04:00, 25 March 2013

Template:STRUCTURE 1b66

6-PYRUVOYL TETRAHYDROPTERIN SYNTHASE

Template:ABSTRACT PUBMED 10024455

Disease

[PTPS_RAT] Note=Deficiency leads to phenylketonuria.

Function

[PTPS_RAT] Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.

About this Structure

1b66 is a 2 chain structure with sequence from Rattus rattus. Full crystallographic information is available from OCA.

Reference

  1. Ploom T, Thony B, Yim J, Lee S, Nar H, Leimbacher W, Richardson J, Huber R, Auerbach G. Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase. J Mol Biol. 1999 Feb 26;286(3):851-60. PMID:10024455 doi:10.1006/jmbi.1998.2511
  2. Colloc'h N, Poupon A, Mornon JP. Sequence and structural features of the T-fold, an original tunnelling building unit. Proteins. 2000 May 1;39(2):142-54. PMID:10737935

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