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- ***************************************************
- * 6-pyruvoyl tetrahydropterin synthase signatures *
- ***************************************************
-
- 6-pyruvoyl tetrahydropterin synthase (EC 4.6.1.10) (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. It forms a homooligomeric
- complex composed of two trimers assembled in a head-to-head fashion. PTPS
- binds a magnesium atom which is liganded by three histidine residues. Three
- residues have been implicated in the catalytic mechanism: a cysteine, an
- histidine and a glutamate.
-
- We have developed two signature patterns for PTPS. The first signature
- contains the active site cysteine and two of the three magnesium ligands. The
- second signature contains the active site histidine.
-
- -Consensus pattern: C-N-N-P-N-G-H-G-H
- [C is an active site residue]
- [The two H's are magnesium ligands]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: D-H-K-N-L-D-x-D
- [H is an active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Last update: June 1994 / First entry.
-
- [ 1] Nar H., Huber R., Heizmann C.W., Thoeny B., Buergisser D.
- EMBO J. 13:1255-1262(1994).
-