Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.13.11.49 extracted from

  • Mlynek, G.; Sjoeblom, B.; Kostan, J.; Fuereder, S.; Maixner, F.; Gysel, K.; Furtmueller, P.G.; Obinger, C.; Wagner, M.; Daims, H.; Djinovic-Carugo, K.
    Unexpected diversity of chlorite dismutases: a catalytically efficient dimeric enzyme from Nitrobacter winogradskyi (2011), J. Bacteriol., 193, 2408-2417.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli strain Tuner (DE3) Nitrobacter winogradskyi

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged enzyme, sitting-drop vapor diffusion technique and a nanodropdispensing robot, from 1.0 M Na2HPO4-NaH2PO4, pH 8.2, at 22°C, 1 week, X-ray diffraction structure determination and analysis at 2.10 A resolution Nitrobacter winogradskyi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten steady-state kinetics, overview Nitrobacter winogradskyi
0.09
-
Chlorite pH 7.0, 30°C, recombinant enzyme Nitrobacter winogradskyi

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Nitrobacter winogradskyi 5737
-
additional information the enzyme does not contain a signal peptide for protein translocation into the periplasm and that the cleaving of a signal peptide at the N terminus would severely disturb the structure of the N-terminal domain Nitrobacter winogradskyi
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ heme enzyme Nitrobacter winogradskyi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
chlorite Nitrobacter winogradskyi
-
chloride + O2
-
?

Organism

Organism UniProt Comment Textmining
Nitrobacter winogradskyi Q3SPU6
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain Tuner (DE3) by nickel affinity chromatography and gel filtration Nitrobacter winogradskyi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chlorite
-
Nitrobacter winogradskyi chloride + O2
-
?

Subunits

Subunits Comment Organism
homodimer subunit interface and active site structures, structure modeling, overview Nitrobacter winogradskyi
More the Cld-like protein from the chemolithoautotrophic nitrite oxidizer Nitrobacter winogradskyi is significantly smaller than all previously known chlorite dismutases Nitrobacter winogradskyi

Synonyms

Synonyms Comment Organism
chlorite dismutase
-
Nitrobacter winogradskyi
CLD
-
Nitrobacter winogradskyi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Nitrobacter winogradskyi

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
190
-
Chlorite pH 7.0, 30°C, recombinant enzyme Nitrobacter winogradskyi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Nitrobacter winogradskyi

Cofactor

Cofactor Comment Organism Structure
heme
-
Nitrobacter winogradskyi

General Information

General Information Comment Organism
additional information despite a truncated N-terminal domain in each subunit, the dimeric enzyme is a highly efficient chlorite dismutase. Subunit interface and active site structures, structure modeling, overview Nitrobacter winogradskyi
physiological function the enzyme detoxifies the chlorite that results from chlorate respiration in bacteria and would otherwise accumulate in the cell and kill the organism. Nitrobacter has a limited chlorite resistance, which enables it to persist and even oxidize nitrite in the presence of low concentrations of chlorate Nitrobacter winogradskyi

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2111
-
Chlorite pH 7.0, 30°C, recombinant enzyme Nitrobacter winogradskyi