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Literature summary for 1.11.1.11 extracted from

  • Gerbling, K.P.; Kelly, G.J.; Fischer, K.H.; Latzko, E.
    Partial purification an properties of soluble ascorbate peroxidases from pea leaves (1984), J. Plant Physiol., 115, 59-67.
    View publication on PubMed
Search for more literature for 1.11.1.11

General Stability

General Stability Organism
loss of activity after incubation of crude extracts from pea shoots with either pronase or chymotrypsin Pisum sativum

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol enzyme form C: 50% inhibition at 5 mM, 6 min, 100% inhibition after 18 min Pisum sativum
dithiothreitol enzyme form C: 100% inhibition at 0.1 mM for 5 min, 57% of the inhibition can be recovered by filtration on Sephadex G-25 and a further 14% is recovered after the addition of homocystine at 2 mM Pisum sativum
KCN enzyme form C: 74% inhibition at 0.1 mM Pisum sativum
NaN3 enzyme form C: 27% inhibition at 5 mM Pisum sativum
reduced glutathione enzyme form C: 75% inhibition at 0.25 mM for 10 min Pisum sativum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information both forms of the enzyme show a very high affinity for H2O2, Km values below 0.005 Pisum sativum
2.9
-
 ascorbate enzyme form C Pisum sativum
6.5
-
 ascorbate enzyme form B Pisum sativum
7.4
-
 guaiacol enzyme form C Pisum sativum

Metals/Ions

Metals/Ions Comment Organism Structure
Fe hemoprotein Pisum sativum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
 crude pea shoot extract, gel filtration, co-elution of two forms of the enzyme, B and C, which can be separated by cation-exchange chromatography Pisum sativum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-ascorbate + H2O2 Pisum sativum physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation dehydroascorbate + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
 pea
-
Pisum sativum
-
 var. Kleine Rheinlaenderin
-

Purification (Commentary)

Purification (Comment) Organism
using Ca-phosphate gel treatment, ammonium sulfate fractionation, column chromatography on Sephadex G-100, ultrafiltration and column chromatography on DEAE-Sephadex and CM-Sephadex C-50, two forms of the enzyme, B and C, can be separated by the CM-Sephadex C-50 step Pisum sativum

Source Tissue

Source Tissue Comment Organism Textmining
shoot
-
 Pisum sativum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
guaiacol + H2O2 form C enzyme, only onesixteenth the rate observed with L-ascorbate Pisum sativum ?
-
 ?
L-ascorbate + H2O2
-
 Pisum sativum dehydroascorbate + H2O
-
 ?
L-ascorbate + H2O2 physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation Pisum sativum dehydroascorbate + 2 H2O
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
 5 min, complete inactivation Pisum sativum
100
-
 10 min, loss of activity Pisum sativum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.2
-
 enzyme form B Pisum sativum
6.2
-
 enzyme form C Pisum sativum

pH Range

pH Minimum pH Maximum Comment Organism
5 8 both forms of the enzyme Pisum sativum

Cofactor

Cofactor Comment Organism Structure
heme
-
 Pisum sativum