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Literature summary extracted from

  • Raedisch, R.; Chmatal, M.; Rucka, L.; Novotny, P.; Petraskova, L.; Halada, P.; Kotik, M.; Patek, M.; Martinkova, L.
    Overproduction and characterization of the first enzyme of a new aldoxime dehydratase family in Bradyrhizobium sp. (2018), Int. J. Biol. Macromol., 115, 746-753 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.8.1.4 Na2S2O4 the addition of Na2S2O4 (5 mM) is essential for the activity of the enzyme Bradyrhizobium sp. LTSPM299

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.8.1.4 expressed in Escherichia coli BL21(DE3) cells Bradyrhizobium sp. LTSPM299
4.8.1.4 expression in Escherichia coli Bradyrhizobium sp. LTSPM299

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.8.1.4 40700
-
 gel filtration Bradyrhizobium sp. LTSPM299

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.8.1.2 an aliphatic aldoxime Pseudomonas chlororaphis
-
 an aliphatic nitrile + H2O
-
 ?
4.8.1.2 an aliphatic aldoxime Pseudomonas chlororaphis B23
-
 an aliphatic nitrile + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.8.1.2 Pseudomonas chlororaphis Q7WSJ4
-
-
4.8.1.2 Pseudomonas chlororaphis B23 Q7WSJ4
-
-
4.8.1.4 Bradyrhizobium sp. LTSPM299 A0A0D7Q864
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.8.1.4 recombinant protein Bradyrhizobium sp. LTSPM299

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.8.1.2 an aliphatic aldoxime
-
 Pseudomonas chlororaphis an aliphatic nitrile + H2O
-
 ?
4.8.1.2 an aliphatic aldoxime
-
 Pseudomonas chlororaphis B23 an aliphatic nitrile + H2O
-
 ?
4.8.1.4 (E/Z)-2-phenylpropionaldoxime 17% of the activity with (E/Z)-phenylacetaldehyde oxime Bradyrhizobium sp. LTSPM299 2-phenylpropiononitrile + H2O
-
 ?
4.8.1.4 (E/Z)-2-phenylpropionaldoxime
-
 Bradyrhizobium sp. LTSPM299 (E/Z)-2-phenylpropiononitrile + H2O
-
 ?
4.8.1.4 (E/Z)-3-phenylpropionaldoxime
-
 Bradyrhizobium sp. LTSPM299 3-phenylpropiononitrile + H2O
-
 ?
4.8.1.4 (E/Z)-3-phenylpropionaldoxime 131% of the activity with (E/Z)-phenylacetaldehyde oxime Bradyrhizobium sp. LTSPM299 3-phenylpropiononitrile + H2O
-
 ?
4.8.1.4 (E/Z)-butyraldoxime
-
 Bradyrhizobium sp. LTSPM299 butyronitrile + H2O
-
 ?
4.8.1.4 (E/Z)-indole-3-acetaldoxime
-
 Bradyrhizobium sp. LTSPM299 indole-3-acetonitrile + H2O
-
 ?
4.8.1.4 (E/Z)-indole-3-acetaldoxime 10% of the activity with (E/Z)-phenylacetaldehyde oxime Bradyrhizobium sp. LTSPM299 indole-3-acetonitrile + H2O
-
 ?
4.8.1.4 (E/Z)-isovaleraldoxime
-
 Bradyrhizobium sp. LTSPM299 isovaleronitrile + H2O
-
 ?
4.8.1.4 (E/Z)-isovaleraldoxime 14% of the activity with (E/Z)-phenylacetaldehyde oxime Bradyrhizobium sp. LTSPM299 isovaleronitrile + H2O
-
 ?
4.8.1.4 (E/Z)-n-butyraldoxime 12% of the activity with (E/Z)-phenylacetaldehyde oxime Bradyrhizobium sp. LTSPM299 n-butyronitrile + H2O
-
 ?
4.8.1.4 (E/Z)-n-valeraldoxime 55% of the activity with (E/Z)-phenylacetaldehyde oxime Bradyrhizobium sp. LTSPM299 n-valeronitrile + H2O
-
 ?
4.8.1.4 (E/Z)-phenylacetaldehyde oxime
-
 Bradyrhizobium sp. LTSPM299 phenylacetonitrile + H2O
-
 ?
4.8.1.4 (E/Z)-phenylacetaldoxime
-
 Bradyrhizobium sp. LTSPM299 phenylacetonitrile + H2O
-
 ?
4.8.1.4 (E/Z)-propionaldoxime
-
 Bradyrhizobium sp. LTSPM299 propionitrile + H2O
-
 ?
4.8.1.4 (E/Z)-propionaldoxime 5% of the activity with (E/Z)-phenylacetaldehyde oxime Bradyrhizobium sp. LTSPM299 propionitrile + H2O
-
 ?
4.8.1.4 (E/Z)-valeraldoxime
-
 Bradyrhizobium sp. LTSPM299 valeronitrile + H2O
-
 ?
4.8.1.4 (Z)-phenylacetaldehyde oxime
-
 Bradyrhizobium sp. LTSPM299 phenylacetonitrile + H2O
-
 ?
4.8.1.4 additional information the enzyme is inactive with (hetero)aromatic aldoximes ((E)-pyridine-2-aldoxime, (E/Z)-pyridine-3-aldoxime, (E/Z)-pyridine-4-aldoxime, and (E/Z)-benzaldoxime) Bradyrhizobium sp. LTSPM299 ?
-
-

Subunits

EC Number Subunits Comment Organism
4.8.1.4 monomer 1 * 40700, calculated from sequence, 1 * 40000, SDS-PAGE, His-tagged recombinant protein Bradyrhizobium sp. LTSPM299
4.8.1.4 monomer 1 * 40000, His6-tagged enzyme, SDS-PAGE Bradyrhizobium sp. LTSPM299
4.8.1.4 monomer 1 * 40700, calculated from amino acid sequence Bradyrhizobium sp. LTSPM299

Synonyms

EC Number Synonyms Comment Organism
4.8.1.2 OxdA
-
 Pseudomonas chlororaphis
4.8.1.4 OxdBr1
-
 Bradyrhizobium sp. LTSPM299
4.8.1.4 UP10_21065
-
 Bradyrhizobium sp. LTSPM299

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.8.1.4 40
-
-
 Bradyrhizobium sp. LTSPM299

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.8.1.4 30
-
 stable up to Bradyrhizobium sp. LTSPM299
4.8.1.4 30
-
 the enzyme is unstable when exposed to temperatures exceeding 30°C Bradyrhizobium sp. LTSPM299

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.8.1.4 7
-
-
 Bradyrhizobium sp. LTSPM299

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.8.1.4 5 7.5
-
 Bradyrhizobium sp. LTSPM299
4.8.1.4 5 7.5 the enzyme is active over a pH range from ca. 5.0 to 7.5 Bradyrhizobium sp. LTSPM299

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.8.1.4 7 8
-
 Bradyrhizobium sp. LTSPM299
4.8.1.4 7 8 the enzyme stability is the highest at pH ca. 7.0-8.0 Bradyrhizobium sp. LTSPM299