Literature summary for 3.6.1.67 extracted from

Gabelli, S.B.; Bianchet, M.A.; Xu, W.; Dunn, C.A.; Niu, Z.D.; Amzel, L.M.; Bessman, M.J.
Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis (2007), Structure, 15, 1014-1022.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure resolved to 1.8 A resolution	Escherichia coli
the structure of the enzyme is determined by X-ray diffraction, 1.8 A resolution. The best crystals grow by microseeding in sitting-drop experiments with a 1 ml reservoir solution of 1.31.5 M ammonium sulfate, 1% propanol, 35 mM DTT, 4 mM sodium diphosphate, 100 mM Na HEPES (pH 6.8). Crystals belong to monoclinic space group C2 with cell dimensions a = 124.1 A, b = 43.2 A, c = 108.0 A, and b = 115.0°	Escherichia coli

Crystallization (Comment)

Organism

crystal structure resolved to 1.8 A resolution

Escherichia coli

the structure of the enzyme is determined by X-ray diffraction, 1.8 A resolution. The best crystals grow by microseeding in sitting-drop experiments with a 1 ml reservoir solution of 1.31.5 M ammonium sulfate, 1% propanol, 35 mM DTT, 4 mM sodium diphosphate, 100 mM Na HEPES (pH 6.8). Crystals belong to monoclinic space group C2 with cell dimensions a = 124.1 A, b = 43.2 A, c = 108.0 A, and b = 115.0°

Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.27	-	7,8-dihydroneopterin 3'-triphosphate	pH 8.5, 37°C	Escherichia coli
0.79	-	dATP	pH 8.5, 37°C	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
7,8-dihydroneopterin 3'-triphosphate + H2O	Escherichia coli	committed step of folate synthesis in bacteria	7,8-dihydroneopterin 3'-phosphate + diphosphate	-	?
7,8-dihydroneopterin 3'-triphosphate + H2O	Escherichia coli	key enzyme in the folate pathway	7,8-dihydroneopterin 3'-phosphate + diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AFC0	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
3	8	pH 8.5, 37°C	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
7,8-dihydroneopterin 3'-triphosphate + H2O	-	Escherichia coli	7,8-dihydroneopterin 3'-phosphate + diphosphate	-	?
7,8-dihydroneopterin 3'-triphosphate + H2O	committed step of folate synthesis in bacteria	Escherichia coli	7,8-dihydroneopterin 3'-phosphate + diphosphate	-	?
7,8-dihydroneopterin 3'-triphosphate + H2O	key enzyme in the folate pathway	Escherichia coli	7,8-dihydroneopterin 3'-phosphate + diphosphate	-	?
dATP + H2O	-	Escherichia coli	dAMP + diphosphate	-	?

Synonyms

Synonyms	Comment	Organism
DHNTPase	-	Escherichia coli
dihydroneopterin triphosphate pyrophosphatase	-	Escherichia coli
nudB	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
4.59	-	dATP	pH 8.5, 37°C	Escherichia coli
11.6	-	7,8-dihydroneopterin 3'-triphosphate	pH 8.5, 37°C	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.5	-	assay at	Escherichia coli

General Information

General Information	Comment	Organism
malfunction	knockout of this gene in Escherichia coli leads to a marked reduction in folate synthesis that is completely restored by a plasmid carrying the gene	Escherichia coli
metabolism	metabolism	Escherichia coli
physiological function	committed step of folate synthesis in bacteria	Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
5.8	-	dATP	pH 8.5, 37°C	Escherichia coli
43	-	7,8-dihydroneopterin 3'-triphosphate	pH 8.5, 37°C	Escherichia coli