Literature summary for 4.2.3.12 extracted from

Woo, H.J.; Hwang, Y.K.; Kim, Y.J.; Kang, J.Y.; Choi, Y.K.; Kim, C.G.; Park, Y.S.
Escherichia coli 6-pyruvoyltetrahydropterin synthase ortholog encoded by ygcM has a new catalytic activity for conversion of sepiapterin to 7,8-dihydropterin (2002), FEBS Lett., 523, 234-238.

Search for more literature for 4.2.3.12

Activating Compound

Activating Compound	Comment	Organism	Structure
EDTA	1-5 mM, 110-120% activation	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
Ca2+	10 mM, 40-100% inhibition	Escherichia coli
Co2+	10 mM, 40-100% inhibition	Escherichia coli
Cu2+	10 mM, 40-100% inhibition	Escherichia coli
EDTA	above 10 mM	Escherichia coli
EDTA	-	Homo sapiens
Mg2+	10 mM, 40-100% inhibition	Escherichia coli
Mn2+	10 mM, 40-100% inhibition	Escherichia coli
Ni2+	10 mM, 40-100% inhibition	Escherichia coli
Zn2+	10 mM, 40-100% inhibition	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.92	-	sepiapterin	pH 7.5, 37ºC	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	no metal ion required	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin	Escherichia coli	the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway	6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate	-	?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin	Homo sapiens	the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway	6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	-	-	-
Escherichia coli	-	-	-
Homo sapiens	-	-	-
Synechocystis sp.	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
extraction, chromatography on a column of Ni-NTA gel	Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.00023	-	SSCR activity	Homo sapiens
0.00034	-	SSCR activity	Drosophila melanogaster
0.00039	-	PTPS activity	Synechocystis sp.
0.00113	-	PTPS activity	Escherichia coli
0.00891	-	PTPS activity	Drosophila melanogaster
0.01303	-	PTPS activity	Homo sapiens
0.09767	-	SSCR activity	Synechocystis sp.
0.09936	-	SSCR activity	Escherichia coli

Storage Stability

Storage Stability	Organism
-70ºC, stable	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin	the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway	Escherichia coli	6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate	-	?
6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin	the enzyme catalyzes the second step in the tetrahydrobiopterin biosynthetic pathway	Homo sapiens	6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate	-	?
sepiapterin	the enzyme cleaves the C6 side chain of sepiapterin, sepiapterin side chain releasing activity, SSCR activity	Escherichia coli	7,8-dihydropterin	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
60	80	3.2fold increase in activity compared to that at 37°C	Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
80	-	-	Homo sapiens
80	-	24% retention of activity after 10 min	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	7	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
additional information	no cofactor required	Escherichia coli

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Release 2023.1 (January 2023)