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Literature summary for 1.11.1.11 extracted from

  • Takeda, T.; Yoshimura, K.; Yoshii, M.; Kanahoshi, H.; Miyasaka, H.; Shigeoka, S.
    Molecular characterization and physiological role of ascorbate peroxidase from halotolerant Chlamydomonas sp. W80 strain (2000), Arch. Biochem. Biophys., 376, 82-90.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, the presence of 3% NaCl as well as beta-D-thiogalactopyranoside is needed for the expression Chlamydomonas sp.

General Stability

General Stability Organism
the enzyme is relatively stable in ascorbate-depleted medium Chlamydomonas sp.

Inhibitors

Inhibitors Comment Organism Structure
KCN complete inhibition at 0.1 mM Chlamydomonas sp.
NaN3 complete inhibition at 4 mM Chlamydomonas sp.
p-chloromercuribenzoate 84% inhibition at 0.2 mM for 5 min Chlamydomonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
H2O2 native and recombinant enzyme Chlamydomonas sp.
0.34
-
ascorbate native and recombinant enzyme Chlamydomonas sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast stroma
-
Chlamydomonas sp. 9570
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30030
-
calculated from the cDNA clone encoding a mature protein of 282 amino acids Chlamydomonas sp.
31000
-
gel filtration, native and recombinant enzyme Chlamydomonas sp.

Organism

Organism UniProt Comment Textmining
Chlamydomonas sp. Q9SXL5 W80 strain
-

Purification (Commentary)

Purification (Comment) Organism
of the native enzyme, using ammonium sulfate precipitation, column chromatography on Phenyl-Sepharose, second ammonium sulfate precipitation, and column chromatography on Superdex 200 and Q Sepharose Chlamydomonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3
-
recombinant enzyme, soluble fraction, addition of 3% NaCl Chlamydomonas sp.
580
-
purified recombinant enzyme Chlamydomonas sp.
636
-
purified native enzyme Chlamydomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cytochrome c + H2O2 no activity Chlamydomonas sp. ? + H2O
-
?
D-iso-ascorbate + H2O2 native enzyme: the activity with D-isoascorbate corresponds to 131% of that found with ascorbate, recombinant enzyme: the activity with D-isoascorbate corresponds to 129% of that found with ascorbate Chlamydomonas sp. dehydroascorbate + H2O
-
?
glutathione + H2O2 no activity Chlamydomonas sp. ? + H2O
-
?
guaiacol + H2O2 native enzyme: the activity corresponds to 7.2% of that found with L-ascorbate, recombinant enzyme: the activity corresponds to 8% of that found with L-ascorbate Chlamydomonas sp. ?
-
?
L-ascorbate + H2O2 native and recombinant enzyme, no activation is observed, when the enzyme is incubated with H2O2 under anaerobic conditions, thus one of the reasons for the stability mechanism in the enzyme may be the insusceptibility of compound I to H2O2 Chlamydomonas sp. dehydroascorbate + H2O
-
?
L-ascorbic acid + cumene hydroperoxide no activity Chlamydomonas sp. dehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
-
?
L-ascorbic acid + tert-butylhydroperoxide no activity Chlamydomonas sp. dehydroascorbate + tert-butylalcohol
-
?
additional information native and recombinant enzyme, no activity with: glutathione, NADPH and cytochrome c Chlamydomonas sp. ?
-
?
NADPH + H2O2 no activity Chlamydomonas sp. ? + H2O
-
?
pyrogallol + H2O2 native enzyme: the activity corresponds to 121% of that found with L-ascorbate, recombinant enzyme: the activity corresponds to 130% of that found with L-ascorbate Chlamydomonas sp. 3-hydroxybenzo-1,2-quinone + H2O
-
?

Subunits

Subunits Comment Organism
monomer 1 * 31000, SDS-PAGE, native and recombinant enzyme Chlamydomonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
42
-
-
Chlamydomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
-
Chlamydomonas sp.
7
-
assay at Chlamydomonas sp.

Cofactor

Cofactor Comment Organism Structure
heme
-
Chlamydomonas sp.