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Literature summary for 3.6.1.1 extracted from

  • Anashkin, V.A.; Orlov, V.N.; Lahti, R.; Baykov, A.A.
    An arginine residue involved in allosteric regulation of cystathionine beta-synthase (CBS) domain-containing pyrophosphatase (2019), Arch. Biochem. Biophys., 662, 40-48 .
    View publication on PubMed
Search for more literature for 3.6.1.1

Activating Compound

Activating Compound Comment Organism Structure
5',5-P1,P4-diadenosine polyphosphate Ap4A, unique as a regulator of CBS-PPase because it bridges two Bateman modules in the dimeric enzyme. It binds non-cooperatively Desulfitobacterium hafniense
ATP
-
 Desulfitobacterium hafniense
additional information inorganic diphosphatase containing a pair of regulatory CBS domains (CBS-PPase1) is allosterically inhibited by AMP and ADP and activated by ATP and diadenosine polyphosphates Desulfitobacterium hafniense

Cloned(Commentary)

Cloned (Comment) Organism
gene AT727_13205, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 Desulfitobacterium hafniense

Protein Variants

Protein Variants Comment Organism
R276A site-directed mutagenesis, the mutant retains about 50% catalytic efficiency compared to wild-type, negative co-operativity is retained in the R276A variant in the presence of mononucleotides but is reversed by diadenosine tetraphosphate. The R276A substitution abolishes activation by ATP and diadenosine tetraphosphate, while preserving the ability to bind them Desulfitobacterium hafniense
R276E site-directed mutagenesis, the mutant retains about 50% catalytic efficiency and exhibits reduced kinetic cooperativity compared to wild-type Desulfitobacterium hafniense
R276K site-directed mutagenesis, the mutant retains about 50% catalytic efficiency and exhibits reduced kinetic cooperativity compared to wild-type Desulfitobacterium hafniense

Inhibitors

Inhibitors Comment Organism Structure
ADP allosteric inhibition Desulfitobacterium hafniense
AMP allosteric inhibition Desulfitobacterium hafniense
additional information inorganic diphosphatase containing a pair of regulatory CBS domains (CBS-PPase1) is allosterically inhibited by AMP and ADP and activated by ATP and diadenosine polyphosphates Desulfitobacterium hafniense

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information mononucleotide binding to CBS domains and substrate binding to catalytic domains are characterized by positive co-operativity, kinetic analysis, overview Desulfitobacterium hafniense

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Desulfitobacterium hafniense 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Desulfitobacterium hafniense

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diphosphate + H2O Desulfitobacterium hafniense
-
 2 phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Desulfitobacterium hafniense A0A098B5G4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + H2O
-
 Desulfitobacterium hafniense 2 phosphate
-
 ?

Synonyms

Synonyms Comment Organism
AT727_13205
-
 Desulfitobacterium hafniense
CBS-PPase1
-
 Desulfitobacterium hafniense
dhPPase
-
 Desulfitobacterium hafniense
inorganic pyrophosphatase
-
 Desulfitobacterium hafniense

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.31
-
 diphosphate pH 7.2, 37°C, wild-type enzyme, in presence of 0.5 mM AMP Desulfitobacterium hafniense
7.2
-
 diphosphate pH 7.2, 37°C, wild-type enzyme, in presence of 0.5 mM ADP Desulfitobacterium hafniense
18
-
 diphosphate pH 7.2, 37°C, mutant R276E, in presence of 0.5 mM AMP Desulfitobacterium hafniense
54
-
 diphosphate pH 7.2, 37°C, mutant R276E, in presence of 0.5 mM ADP Desulfitobacterium hafniense
58
-
 diphosphate pH 7.2, 37°C, mutant R276A, in presence of 0.5 mM AMP Desulfitobacterium hafniense
88
-
 diphosphate pH 7.2, 37°C, mutant R276A, in presence of 0.5 mM ADP Desulfitobacterium hafniense
112
-
 diphosphate pH 7.2, 37°C, mutant R276A, in presence of 0.5 mM Ap4A Desulfitobacterium hafniense
115
-
 diphosphate pH 7.2, 37°C, mutant R276A, in presence of 0.5 mM ATP Desulfitobacterium hafniense
120
-
 diphosphate pH 7.2, 37°C, mutant R276E, in presence of 0.5 mM ATP Desulfitobacterium hafniense
173
-
 diphosphate pH 7.2, 37°C, mutant R276K, in presence of 0.5 mM ATP Desulfitobacterium hafniense
215
-
 diphosphate pH 7.2, 37°C, mutant R276K, in presence of 0.5 mM Ap4A Desulfitobacterium hafniense
225
-
 diphosphate pH 7.2, 37°C, wild-type enzyme, in presence of 0.5 mM ATP Desulfitobacterium hafniense
240
-
 diphosphate pH 7.2, 37°C, mutant R276E, in presence of 0.5 mM Ap4A Desulfitobacterium hafniense
308
-
 diphosphate pH 7.2, 37°C, wild-type enzyme, in presence of 0.5 mM Ap4A Desulfitobacterium hafniense

pH Optimum

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

General Information

General Information Comment Organism
additional information inorganic diphosphatase containing a pair of regulatory CBS domains (CBS-PPase1) is allosterically inhibited by AMP and ADP and activated by ATP and diadenosine polyphosphatesegulated involving residue Arg276 at the interface of the regulatory and catalytic domains of CBS-PPase1, overview. The H-bond formed by the Arg276 sidechain is essential for signal transduction between the regulatory and catalytic domains within one subunit and between the catalytic but not regulatory domains of different subunits Desulfitobacterium hafniense