Information on EC 4.1.2.50 - 6-carboxytetrahydropterin synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.1.2.50
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RECOMMENDED NAME
GeneOntology No.
6-carboxytetrahydropterin synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Folate biosynthesis
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Metabolic pathways
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preQ0 biosynthesis
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tetrahydrofolate metabolism
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SYSTEMATIC NAME
IUBMB Comments
7,8-dihydroneopterin 3'-triphosphate acetaldehyde-lyase (6-carboxy-5,6,7,8-tetrahydropterin and triphosphate-forming)
Binds Zn2+. Isolated from the bacteria Bacillus subtilis and Escherichia coli. The reaction is part of the biosynthesis pathway of queuosine.The enzyme from Escherichia coli can also convert 6-pyruvoyl-5,6,7,8-tetrahydropterin and sepiapterin to 6-carboxy-5,6,7,8-tetrahydropterin [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene queD
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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QueD is one of several enzymes involved in the biosynthesis of the hypermodified nucleoside queuosine. Formation of queuosine is a multistep reaction that can be divided into three stages, overview
physiological function
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QueD catalyzes the conversion of 7,8-dihydroneopterin triphosphate to 6-carboxy-5,6,7,8-tetrahydropterin, CPH4. QueD can also convert 6-pyruvoyltetrahydropterin, PPH4, and sepiapterin to CPH4
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-pyruvoyltetrahydropterin + H2O
6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate
show the reaction diagram
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?
7,8-dihydroneopterin triphosphate + H2O
6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate
show the reaction diagram
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?
sepiapterin + H2O
6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate
show the reaction diagram
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additional information
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6-pyruvoyltetrahydropterin can tautomerize to sepiapterin, the hydrate of which undergoes carbon-carbon bond cleavage by an aldolase-like mechanism, followed by a tautomerization, to yield 6-carboxy-5,6,7,8-tetrahydropterin
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recomb inant QueD, hanging-drop vapor-diffusion method, mixing of 800 nl of protein solution containing 10 mg/ml protein and of 800 nl crystallization solution containing 25% PEG 600, 100 mM NaCl and sodium citrate buffer, pH 5.5, at 18°C, X-ray diffraction structure determination and analysis at 3.6 A resolution
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crystal structures of wild-type apo 6-carboxytetrahydropterin synthase and of a C27A mutant complexed with sepiapterin to 2.3 and 2.5 A resolution, respectively. The structures are highly conserved at the active site and the Zn2+ binding site. Residues Trp51 and Phe55, that are not found in mammalian 6-pyruvoyltetrahydropterin synthase keep the substrate bound by stacking it with their side chains. Replacement of these two residues by site-directed mutagenesis to the residues Met and Leu, which are only found in mammalian 6-pyruvoyltetrahydropterin synthase, converted the enzyme to the mammalian 6-pyruvoyltetrahydropterin synthase activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant QueD from Escherichia coli strain BL21 (DE3) by anion exchange and hydrophobic inetraction chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene queD, overexpression in Escherichia coli strain BL21 (DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C27A
significant decrease in catalytic activity
F55L
mutants shows 6-pyruvoyltetrahydropterin synthase activities comparable to the mammalian enzymes, with concomitant decrease in 6-carboxytetrahydropterin synthase activity
W51M
mutants shows 6-pyruvoyltetrahydropterin synthase activities comparable to the mammalian enzymes, with concomitant decrease in 6-carboxytetrahydropterin synthase activity
W51M/F55L
mutants shows 6-pyruvoyltetrahydropterin synthase activities comparable to the mammalian enzymes, with concomitant decrease in 6-carboxytetrahydropterin synthase activity
Show AA Sequence (183 entries)
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