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Literature summary for 1.2.3.4 extracted from

  • Chauhan, N.; Hooda, V.; Pundir, C.
    In vitro effects of metal oxide nanoparticles on barley oxalate oxidase (2013), J. Nanopart. Res., 15, 1493.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
diethyldithiocarbamate 35% increase of activity at 1 mM Hordeum vulgare
DW 1750000 21% increase of activity at 1 mM Hordeum vulgare
additional information compared to free enzyme, MnO2 nanoparticles(NP)-bound enzyme shows improved activity (35% stimulation at 2.5 mg/ml) while ZnO NPs- and CuO NPs-bound enzymes have no substantial improvement Hordeum vulgare

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 92% residual activity at 1 mM Hordeum vulgare
K+ 94% residual activity at 1 mM Hordeum vulgare
additional information not influenced by EDTA, NaCl, and MgSO4 Hordeum vulgare
NEM 92% residual activity at 1 mM Hordeum vulgare
Sodium azide 86% residual activity at 1 mM Hordeum vulgare
Sodium molybdate 71% residual activity at 1 mM Hordeum vulgare
Sodium nitrate 45% residual activity at 1 mM Hordeum vulgare
sodium thiocyanate 72% residual activity at 1 mM Hordeum vulgare
ZnSO4 90% residual activity at 1 mM Hordeum vulgare

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ 21% increase of activity at 1 mM Hordeum vulgare
Fe2+ 10% increase of activity at 1 mM Hordeum vulgare
Mn2+ 37% increase of activity at 1 mM Hordeum vulgare

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
oxalate + O2 + H+ Hordeum vulgare
-
CO2 + H2O2
-
?
oxalate + O2 + H+ Hordeum vulgare BH393
-
CO2 + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
-
-
-
Hordeum vulgare BH393
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-Sephacel column chromatography and Sephadex G-100 gel filtration Hordeum vulgare

Source Tissue

Source Tissue Comment Organism Textmining
root
-
Hordeum vulgare
-

Storage Stability

Storage Stability Organism
4-8°C, 90 days, native enzyme, up to 70% loss of activity Hordeum vulgare

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxalate + O2 + H+
-
Hordeum vulgare CO2 + H2O2
-
?
oxalate + O2 + H+
-
Hordeum vulgare BH393 CO2 + H2O2
-
?

Synonyms

Synonyms Comment Organism
oxalate: O2 oxidoreductase
-
Hordeum vulgare
OXO
-
Hordeum vulgare

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
nanoparticle-bound enzyme Hordeum vulgare
40
-
free enzyme Hordeum vulgare

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
metal oxide nanoparticles(NP)-bound enzyme retains more activity when subjected to thermal treatment at 70°C for 30 min., retention of activity in the increasing order being 54%, 65%, 76%, and 87% for native, ZnO NPs-, CuO NPs-, and MnO2 NPs-bound enzyme, respectively Hordeum vulgare

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2
-
free enzyme Hordeum vulgare
4
-
nanoparticle-bound enzyme Hordeum vulgare

Cofactor

Cofactor Comment Organism Structure
additional information FMN, FAD, NAD+, and riboflavin at 1 mM in the presence of nanoparticles have practically no effect on native and immobilized enzymes Hordeum vulgare