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Literature summary extracted from

  • Van, R.C.; Pan, Y.J.; Hsu, S.H.; Huang, Y.T.; Hsiao, Y.Y.; Pan, R.L.
    Role of transmembrane segment 5 of the plant vacuolar H+-pyrophosphatase (2005), Biochim. Biophys. Acta, 1709, 84-94.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.1 subcloning in Escherichia coli strain XL1-blue, expression of wild-type and mutant enzymes in enzyme-deficient Saccharomyces cerevisiae strain BJ268 Vigna radiata

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.1 A226S site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 A238S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 E225A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 F224A site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 F240A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 G221A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 G222A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 G229A site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 G231A site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 G233A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 G234A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 G241A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 I227A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 L223A site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 L232A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 L239A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 M237A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 R242A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 S235A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 S236A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 T228A site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme Vigna radiata
3.6.1.1 Y230A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Vigna radiata

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.1 Ca2+
-
 Vigna radiata
3.6.1.1 F-
-
 Vigna radiata
3.6.1.1 Na+
-
 Vigna radiata

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.1 additional information
-
 additional information kinetics of wild-type and mutant enzymes Vigna radiata
3.6.1.1 0.008
-
 diphosphate pH 8.0, 37°C, mutant Y230A Vigna radiata
3.6.1.1 0.016
-
 diphosphate pH 8.0, 37°C, mutant G231A Vigna radiata
3.6.1.1 0.022
-
 diphosphate pH 8.0, 37°C, mutant R242A Vigna radiata
3.6.1.1 0.035
-
 diphosphate pH 8.0, 37°C, mutant L232A Vigna radiata
3.6.1.1 0.054
-
 diphosphate pH 8.0, 37°C, mutant E225A Vigna radiata
3.6.1.1 0.068
-
 diphosphate pH 8.0, 37°C, mutant G229A Vigna radiata
3.6.1.1 0.07
-
 diphosphate pH 8.0, 37°C, mutant G234A Vigna radiata
3.6.1.1 0.074
-
 diphosphate pH 8.0, 37°C, mutant G233A Vigna radiata
3.6.1.1 0.099
-
 diphosphate pH 8.0, 37°C, mutant F240A Vigna radiata
3.6.1.1 0.105
-
 diphosphate pH 8.0, 37°C, mutant S236A Vigna radiata
3.6.1.1 0.112
-
 diphosphate pH 8.0, 37°C, mutant M237A Vigna radiata
3.6.1.1 0.14
-
 diphosphate pH 8.0, 37°C, mutant I227A Vigna radiata
3.6.1.1 0.146
-
 diphosphate pH 8.0, 37°C, mutant T228A Vigna radiata
3.6.1.1 0.148
-
 diphosphate pH 8.0, 37°C, mutant G221A Vigna radiata
3.6.1.1 0.154
-
 diphosphate pH 8.0, 37°C, wild-type enzyme Vigna radiata
3.6.1.1 0.185
-
 diphosphate pH 8.0, 37°C, mutant A226S Vigna radiata
3.6.1.1 0.196
-
 diphosphate pH 8.0, 37°C, mutant A238S Vigna radiata
3.6.1.1 0.199
-
 diphosphate pH 8.0, 37°C, mutant S235A Vigna radiata
3.6.1.1 0.221
-
 diphosphate pH 8.0, 37°C, mutant L239A Vigna radiata
3.6.1.1 0.305
-
 diphosphate pH 8.0, 37°C, mutant F224A Vigna radiata
3.6.1.1 0.318
-
 diphosphate pH 8.0, 37°C, mutant G222A Vigna radiata
3.6.1.1 0.332
-
 diphosphate pH 8.0, 37°C, mutant G241A Vigna radiata
3.6.1.1 0.438
-
 diphosphate pH 8.0, 37°C, mutant L223A Vigna radiata

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.1 vacuolar membrane the enzyme contains several transmembrane segments Vigna radiata 5774
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.1 K+ required, highly activating Vigna radiata
3.6.1.1 Mg2+ required Vigna radiata

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.1 81000
-
-
 Vigna radiata

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.1 diphosphate + H2O Vigna radiata
-
 2 phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.1 Vigna radiata
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.1 diphosphate + H2O
-
 Vigna radiata 2 phosphate
-
 ?
3.6.1.1 additional information the enzyme acts as diphosphate-dependent H+-translocation pump Vigna radiata ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.1.1 dimer the homodimer contains several transmembrane segments, the conserved transmembrane segment 5 at the N-terminal side near the putative substrate binding loop contains the GYG motif which is important in maintaining structure and function of the enzyme, overview Vigna radiata

Synonyms

EC Number Synonyms Comment Organism
3.6.1.1 V-PPase
-
 Vigna radiata
3.6.1.1 vacuolar H+-pyrophosphatase
-
 Vigna radiata
3.6.1.1 vacuolar H+-translocating inorganic pyrophosphatase
-
 Vigna radiata

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.1 37
-
 assay at Vigna radiata

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.1 7.4 8.1 pH optima of mutant enzymes, overview Vigna radiata
3.6.1.1 8
-
 pH optimum of the wild-type enzyme Vigna radiata