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Information on EC 4.2.3.12 - 6-pyruvoyltetrahydropterin synthase
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EC Tree
4.2.3.12 6-pyruvoyltetrahydropterin synthaseIUBMB Comments
Catalyses triphosphate elimination and an intramolecular redox reaction in the presence of Mg2+. It has been identified in human liver. This enzyme is involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 (sepiapterin reductase) and EC 3.5.4.16 (GTP cyclohydrolase I) .
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Word Map
- 4.2.3.12
- phosphatases
-
protein-tyrosine
- phosphotyrosine
- src
- hyperphenylalaninemia
- bh4
- sepiapterin
- orthovanadate
-
dual-specificity
-
cyclohydrolase
- tcptp
- dihydropteridine
- vanadate
-
receptor-like
-
receptor-type
-
phenylarsine
-
rfviii
- pterins
- ptp-pest
- ptp-1b
- 5-hydroxytryptophan
-
sulfenic
- pteridines
- ptpalpha
-
phosphotyrosyl
-
tyrosine-specific
-
thoracotomy
- phenylketonuria
- medicine
- ptpro
- gtpch
- haemophilia
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substrate-trapping
- dystonia
- pervanadate
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non-receptor
- csk
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antigen-related
- ptpn22
- cdc25
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
ptps, 6-pyruvoyl-tetrahydropterin synthase, 6-pyruvoyltetrahydropterin synthase, ptp synthase, eptps, ptps-iii, pyruvoyltetrahydropterin synthase, sco 6650, 6-pyruvoyl tetrahydrobiopterin synthase, ph0634, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-amino-4-oxo-6-(erythro-1',2',3'-trihydroxypropyl)-7,8-dihydroxypterdine triphosphate lyase
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6-(1,2-dioxopropyl)tetrahydropterin synthase
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6-carboxy-5,6,7,8-tetrahydropterin synthase
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6-pyruvoyl-5,6,7,8-tetrahydropterin synthase homologue, gene QueD
6-pyruvoyl-tetrahydropterin synthase
6-pyruvoyltetrahydropterin synthase
6-pyruvoyltetrahydropterin synthase paralog
6-pyruvoyltetrahydropterin synthase [16-cysteine] (human clone lamda HSY2 gene PCBD subunit)
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6-pyruvoyltetrahydropterin synthase [25-glutamine] (human clone lambdaHSY2 gene PCBD subunit)
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6-pyruvoyltetrahydropterin synthase [de-57-valine] (human clone lambdaHSY2 gene PCBD subunit)
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6-pyruvoyltetrahydropterin synthase-like protein
EC 4.6.1.10
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formerly
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PPH4 synthase
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PPH4S
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protein purple
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PTP synthase
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PTPS
PTPS-III
pyruvoyltetrahydropterin synthase
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synthase, 6-pyruvoyltetrahydropterin
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synthase, 6-pyruvoyltetrahydropterin [16-cysteine] (human clone lamda HSY2 gene PCBD subunit)
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synthase, 6-pyruvoyltetrahydropterin [25-glutamine] (human clone lamdaHSY2 gene PCBD subunit)
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synthase, 6-pyruvoyltetrahydropterin [87-leucine] (human clone lamdaHSY2 gene PCBD subunit)
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synthase, 6-pyruvoyltetrahydropterin [de-57-valine] (human clone lambdaHSY2 gene PCBD subunit)
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6-pyruvoyltetrahydropterin synthase
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PTPS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
mechanism
-
7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
the enzyme catalyzes the elimination of triphosphate as well as a series of tautomerization reactions. Incorporation of protons into positions C6 and C3' of the product
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7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
catalyses triphosphate elimination and an intramolecular redox reaction in the presence of Mg2+. Identified in human liver. The product is 6-pyruvoyltetrahydrobiopterin
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cleavage of triphosphate bond
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intramolecular redox reaction
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P-O bond cleavage
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triphosphate elimination
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
7,8-dihydroneopterin 3'-triphosphate triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming)
Catalyses triphosphate elimination and an intramolecular redox reaction in the presence of Mg2+. It has been identified in human liver. This enzyme is involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 (sepiapterin reductase) and EC 3.5.4.16 (GTP cyclohydrolase I) [3].
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CAS REGISTRY NUMBER
COMMENTARY
171716-27-1
synthase, 6-pyruvoyltetrahydropterin [16-cysteine] (human clone lamda HSY2 gene PCBD subunit) /6-pyruvoyltetrahydropterin synthase [16-cysteine] (human clone lambda HSY2 gene PCBD subunit)
171716-28-2
synthase, 6-pyruvoyltetrahydropterin [25-glutamine] (human clone lambdaHSY2 gene PCBD subunit) /6-pyruvoyltetrahydropterin synthase [25-glutamine] (human clone lambdaHSY2 gene PCBD subunit)
171716-29-3
synthase, 6-pyruvoyltetrahydropterin [de-57-valine] (human clone lambdaHSY2 gene PCBD subunit) /6-pyruvoyltetrahydropterin synthase [de-57-valine] (human clone lambdaHSY2 gene PCBD subunit)
171716-30-6
synthase, 6-pyruvoyltetrahydropterin [87-leucine] (human clone lambdaHSY2 gene PCBD subunit)
97089-82-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1'-3H-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
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tritium released is not incorporated in the product
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?
2'-3H-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
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tritium released is not incorporated in the product
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?
6-(L-erythro-1,2-dihydroxypropyl 3-monophosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + monophosphate
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the binding constant is 225fold increased with respect to the natural substrate
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
?
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the second of the three enzymatic steps in the synthesis of tetrahydrobiopterin from GTP
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?
7,8-dihydroneopterin 3'-triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
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?
additional information
?
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the sequence of reaction steps include redox transfer between atoms N5, C6 and C1' and unusual triphosphate elimination at the C2'-C3' bond in the side chain
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
23 bp exon 3 skipping in transcription rather than post-transcriptional mechanisms is a major cause of the low PTPS protein expression in human macrophages and related cell types. The exon lacking leads to a premature stop codon encoding for a shorter protein instead of the full-length functional enzyme
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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rate-limiting enzyme in the synthesis of human tetrahydrobiopterin
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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the enzyme catalyzes the first step in the conversion of 7,8-dihydroneopterin triphosphate to tetrahydrobiopterin
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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the enzyme is involved in tetrahydrobiopterin biosynthesis
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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the enzyme is post-translationally phosphorylated in several Ser residues by protein kinases. The enzyme requires the phosphoserine 19 residue for maximal activity under in vivo conditions. Mutant enzymes with alterations in the protein kinase recognition site, phosphoserine 19 residue, are not phosphorylated by protein kinase and have reduced activity
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme is involved in tetrahydrobiopterin biosynthesis
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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the enzyme has six active sites located at the interface of three subunits. The enzyme contains an intersubunit catalytic triad motif composed of the amino acid residues Cys A42, His B89 and Asp B88 which is involved in the abstraction of protons from the substrate side-chain carbons. The gamma and beta phosphates of the substrate are essential for substrate binding and enhance the catalytic efficiency
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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-
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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one of the enzymes involved in tetrahydrobiopterin biosynthesis
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?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
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the enzyme catalyzes the second step of tetrahydrobiopterin (BH4) synthesis
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-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
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-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
dihydroneopterin triphosphate
6-hydroxymethyldihydropterin + triphosphate + ?
-
-
-
-
?
dihydroneopterin triphosphate
6-hydroxymethyldihydropterin + triphosphate + ?
-
-
-
-
?
sepiapterin
7,8-dihydropterin
-
the enzyme cleaves the C6 side chain of sepiapterin, sepiapterin side chain releasing activity, SSCR activity
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
?
-
the second of the three enzymatic steps in the synthesis of tetrahydrobiopterin from GTP
-
-
?
7,8-dihydroneopterin 3'-triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
additional information
?
-
-
the sequence of reaction steps include redox transfer between atoms N5, C6 and C1' and unusual triphosphate elimination at the C2'-C3' bond in the side chain
-
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
23 bp exon 3 skipping in transcription rather than post-transcriptional mechanisms is a major cause of the low PTPS protein expression in human macrophages and related cell types. The exon lacking leads to a premature stop codon encoding for a shorter protein instead of the full-length functional enzyme
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
rate-limiting enzyme in the synthesis of human tetrahydrobiopterin
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme catalyzes the first step in the conversion of 7,8-dihydroneopterin triphosphate to tetrahydrobiopterin
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme is involved in tetrahydrobiopterin biosynthesis
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme is post-translationally phosphorylated in several Ser residues by protein kinases. The enzyme requires the phosphoserine 19 residue for maximal activity under in vivo conditions. Mutant enzymes with alterations in the protein kinase recognition site, phosphoserine 19 residue, are not phosphorylated by protein kinase and have reduced activity
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme is involved in tetrahydrobiopterin biosynthesis
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme has six active sites located at the interface of three subunits. The enzyme contains an intersubunit catalytic triad motif composed of the amino acid residues Cys A42, His B89 and Asp B88 which is involved in the abstraction of protons from the substrate side-chain carbons. The gamma and beta phosphates of the substrate are essential for substrate binding and enhance the catalytic efficiency
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
one of the enzymes involved in tetrahydrobiopterin biosynthesis
-
?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
-
the enzyme catalyzes the second step of tetrahydrobiopterin (BH4) synthesis
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
-
-
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
7,8-dihydroneopterin triphosphate
6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
-
assay at
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
-
free metal enzyme activity reaches 60% of activity of wild type with 0.50 mM and concentrations higher than 0.15 mM completely inactivates the enzyme. Less than 15% of activity with Mg2+ with 5 mM
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Mg2+
-
free metal enzyme activity is 15% of the wild type with 8 mM, it is not bound to the enzyme
Zn2+
-
free metal enzyme activity reaches 85% of activity of wild type with 0.05 mM and 8 mM Mg2+
Zn2+
bound to the Nepsilon-atoms of the three His residues HisA23, HisA48, and HisA50, one to each of the two active sites
Zn2+
-
concentrations higher than 0.15 mM completely inactivates the enzyme
additional information
-
Cu2+, Fe2+, less than 15% of activity with Mg2+ with 5 mM of each ion
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-Vinylpyridine
-
95% inactivation under non-denaturating and non-reducing conditions
4-Vinylpyridine
-
80% inactivation under non-denaturating and non-reducing conditions
additional information
NaCl 100 mM and KCl 100 mM have no effect on activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE