{PDOC00759}
{PS00987; PTPS_1}
{PS00988; PTPS_2}
{BEGIN}
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* 6-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.

-Consensus pattern: C-N-N-x(2)-G-H-G-H-N-Y
                    [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,  except
 for E.coli PTPS.
-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,  except
 for E.coli and C.elegans PTPS.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: November 1997 / Patterns and text revised.

[ 1] Nar H., Huber R., Heizmann C.W., Thoeny B., Buergisser D.
     "Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase,
     an enzyme involved in tetrahydrobiopterin biosynthesis."
     EMBO J. 13:1255-1262(1994).
     PubMed=8137809

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