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Literature summary extracted from

  • Nnamchi, C.I.; Parkin, G.; Efimov, I.; Basran, J.; Kwon, H.; Svistunenko, D.A.; Agirre, J.; Okolo, B.N.; Moneke, A.; Nwanguma, B.C.; Moody, P.C.; Raven, E.L.
    Structural and spectroscopic characterisation of a heme peroxidase from sorghum (2016), J. Biol. Inorg. Chem., 21, 63-70 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.11.1.7 Ca2+ about 8fold increase in kcat value in presence of Ca2+ Sorghum bicolor

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.7 to 1.27 A resolution. Metal binding sites are observed in the structure on the distal (assigned as a Na+ ion) and proximal (assigned as a Ca2+) sides of the heme Sorghum bicolor

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.7 1.6
-
H2O2 pH 5.5, 25°C Sorghum bicolor
1.11.1.7 1.6
-
H2O2 presence of Ca2+, pH 5.5, 25°C Sorghum bicolor

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.7 Iron enzyme contains a high-spin heme. The FeIII/FeII reduction potential is -266 mV vs normal hydrogen electrode. The ferric enzyme binds cyanide or azide to give a low-spin species Sorghum bicolor

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.7 Sorghum bicolor
-
-
-
1.11.1.7 Sorghum bicolor SK 5912
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.7
-
Sorghum bicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.7 2 guaiacol + H2O2 27% of the activity with 2,4-dichlorophenol Sorghum bicolor 3,3'-dimethoxy-4,4'-biphenylquinone + H2O
-
?
1.11.1.7 2 guaiacol + H2O2 27% of the activity with 2,4-dichlorophenol Sorghum bicolor SK 5912 3,3'-dimethoxy-4,4'-biphenylquinone + H2O
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.11.1.7 9.9
-
H2O2 pH 5.5, 25°C Sorghum bicolor
1.11.1.7 87
-
H2O2 presence of Ca2+, pH 5.5, 25°C Sorghum bicolor

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.7 heme enzyme contains a high-spin heme. The FeIII/FeII reduction potential is -266 mV vs normal hydrogen electrode. The gamma-heme edge shows a substrate binding site Sorghum bicolor