PROSITE documentation PDOC00759
6-pyruvoyl tetrahydropterin synthase signatures


6-pyruvoyl tetrahydropterin synthase (EC (PTPS) [1] catalyzes the second step in the biosynthesis of tetrahydrobiopterin (BH4); a complex rearrangement of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.

PTPS is a small protein of about 145 residues and forms a homooligomeric complex of two trimers assembled in a head-to-head fashion. It binds a magnesium atom which is ligated by three histidine residues. Three residues are implicated in the catalytic mechanism: a cysteine, a histidine and a glutamate.

We developed two signature patterns for PTPS. The first contains the active site cysteine and two of the three magnesium ligands. The second signature contains the active site histidine.

Last update:

November 1997 / Patterns and text revised.


Technical section

PROSITE methods (with tools and information) covered by this documentation:

PTPS_1, PS00987; 6-pyruvoyl tetrahydropterin synthase signature 1  (PATTERN)

PTPS_2, PS00988; 6-pyruvoyl tetrahydropterin synthase signature 2  (PATTERN)


1AuthorsNar H. Huber R. Heizmann C.W. Thoeny B. Buergisser D.
TitleThree-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis.
SourceEMBO J. 13:1255-1262(1994).
PubMed ID8137809

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