PROSITE documentation PDOC007596-pyruvoyl tetrahydropterin synthase signatures
6-pyruvoyl tetrahydropterin synthase (EC 4.2.3.12) (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.
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| 1 | Authors | Nar H. Huber R. Heizmann C.W. Thoeny B. Buergisser D. |
| Title | Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis. | |
| Source | EMBO J. 13:1255-1262(1994). | |
| PubMed ID | 8137809 |
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