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Literature summary for 3.6.1.1 extracted from

  • Anashkin, V.A.; Salminen, A.; Vorobjeva, N.N.; Lahti, R.; Baykov, A.A.
    An asparagine residue mediates intramolecular communication in nucleotide-regulated pyrophosphatase (2016), Biochem. J., 473, 2097-2107 .
    View publication on PubMed
Search for more literature for 3.6.1.1

Protein Variants

Protein Variants Comment Organism
additional information naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics Ethanoligenens harbinense
additional information naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics Desulfitobacterium hafniense
N312S site-directed mutagenesis, the mutant shows altered Mg2+ dependence and kinetics compared to wild-type. The N312S substitution in dhPPase abolishes kinetic cooperativity and reverses the effect of Ap4A on it. In the presence of 0.05 mMATP and 5 mM Mg2+, the hydrolysis kinetics of N312S-dhPPase remains non-cooperative, the catalytic constant increases 1.5fold, and the average Km value increases about 5.5fold Desulfitobacterium hafniense
S213N site-directed mutagenesis, the substitution confers significant negative cooperativity on the enzyme, decreasing the Hill coefficient to 0.7, and the Km2/Km1 ratio increases to approximately 13 over the entire range of Mg2+ concentrations. The catalytic constant decreases by a factor of 4.5 upon Ser213 replacement Ethanoligenens harbinense

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information ehPPase lacks kinetic cooperativity, kinetic analysis, Michaelis-Menten kinetics, overview. The S213N substitution conferred significant negative cooperativity on the enzyme, decreasing the Hill coefficient to 0.7, and the Km2/Km1 ratio increases to approximately 13 over the entire range of Mg2+ concentrations Ethanoligenens harbinense
additional information
-
 additional information kinetic analysis, Michaelis-Menten kinetics, overview. With the wild-type enzyme, hydrolysis kinetics remains positively cooperative in the presence of ATP Desulfitobacterium hafniense
0.049 0.097 diphosphate pH 7.2, 25°C, mutant enzyme N312S Desulfitobacterium hafniense
0.6
-
 diphosphate pH 7.2, 25°C, wild-type enzyme Desulfitobacterium hafniense
35
-
 diphosphate pH 7.2, 25°C, mutant enzyme S213N Ethanoligenens harbinense
46
-
 diphosphate pH 7.2, 25°C, wild-type enzyme Ethanoligenens harbinense

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Ethanoligenens harbinense
-
-
soluble
-
 Desulfitobacterium hafniense
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ required Ethanoligenens harbinense
Co2+ required Desulfitobacterium hafniense
Mg2+ dependent on Desulfitobacterium hafniense
Mg2+ dependent on, Mg2+ concentration-dependence of kinetic cooperativity in wild-type ehPPase and mutant S213N-ehPPase, overview Ethanoligenens harbinense
Mn2+ required Ethanoligenens harbinense
Mn2+ required Desulfitobacterium hafniense

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diphosphate + H2O Ethanoligenens harbinense
-
 2 phosphate
-
 r
diphosphate + H2O Desulfitobacterium hafniense
-
 2 phosphate
-
 r
diphosphate + H2O Desulfitobacterium hafniense DSM 10664
-
 2 phosphate
-
 r
diphosphate + H2O Desulfitobacterium hafniense DCB-2
-
 2 phosphate
-
 r
diphosphate + H2O Ethanoligenens harbinense UniProt
-
 2 phosphate
-
 r

Organism

Organism UniProt Comment Textmining
Desulfitobacterium hafniense B8FP42
-
-
Desulfitobacterium hafniense DCB-2 B8FP42
-
-
Desulfitobacterium hafniense DSM 10664 B8FP42
-
-
Ethanoligenens harbinense E6U5H4
-
-
Ethanoligenens harbinense UniProt E6U5H4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + H2O
-
 Ethanoligenens harbinense 2 phosphate
-
 r
diphosphate + H2O
-
 Desulfitobacterium hafniense 2 phosphate
-
 r
diphosphate + H2O
-
 Desulfitobacterium hafniense DSM 10664 2 phosphate
-
 r
diphosphate + H2O
-
 Desulfitobacterium hafniense DCB-2 2 phosphate
-
 r
diphosphate + H2O
-
 Ethanoligenens harbinense UniProt 2 phosphate
-
 r

Subunits

Subunits Comment Organism
homodimer
-
 Ethanoligenens harbinense
homodimer
-
 Desulfitobacterium hafniense

Synonyms

Synonyms Comment Organism
dhPPase
-
 Desulfitobacterium hafniense
ehPPase
-
 Ethanoligenens harbinense
nucleotide-regulated pyrophosphatase
-
 Ethanoligenens harbinense
nucleotide-regulated pyrophosphatase
-
 Desulfitobacterium hafniense
PPase
-
 Ethanoligenens harbinense
PPase
-
 Desulfitobacterium hafniense
pyrophosphatase
-
 Ethanoligenens harbinense
pyrophosphatase
-
 Desulfitobacterium hafniense

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Ethanoligenens harbinense
25
-
 assay at Desulfitobacterium hafniense

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
10
-
 diphosphate pH 7.2, 25°C, mutant enzyme S213N Desulfitobacterium hafniense
320
-
 diphosphate pH 7.2, 25°C, wild-type enzyme Desulfitobacterium hafniense
410
-
 diphosphate pH 7.2, 25°C, mutant enzyme S213N Ethanoligenens harbinense
1850
-
 diphosphate pH 7.2, 25°C, wild-type enzyme Ethanoligenens harbinense

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Ethanoligenens harbinense
7.2
-
 assay at Desulfitobacterium hafniense

General Information

General Information Comment Organism
evolution the enzyme belongs to the CBS-PPases Ethanoligenens harbinense
evolution the enzyme belongs to the CBS-PPases Desulfitobacterium hafniense
malfunction naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics Ethanoligenens harbinense
malfunction naturally occuring ehPPase mutant containing an inherent mutation in an otherwise conserved asparagine residue in a loop near the active site exhibits noncooperative hydrolysis kinetics Desulfitobacterium hafniense
additional information comparison of the primary structure of ehPPase with those of five other CBS-PPases. Molecular dynamic simulations, overview Ethanoligenens harbinense
additional information structure comparisons of CBS-PPases and molecular dynamic simulations, overview Desulfitobacterium hafniense
physiological function ehPPase lacks kinetic cooperativity and is not regulated by adenine nucleotides. ehPPase shows insensitivity (below 10% activity change) to adenine nucleotides (AMP, ADP, ATP and diadenosine polyphosphates, ApnA, with n=3-6) over a wide range of substrate concentrations (0.001-0.30 mM), metal cofactor concentrations (0.05-20 mM), and nucleotide concentrations (10 nM-1.0 mM) for mononucleotides and 0.01 nM-0.1 mM for dinucleotides Ethanoligenens harbinense