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Literature summary extracted from

  • Dicko, M.H.; Gruppen, H.; Hilhorst, R.; Voragen, A.G.; van Berkel, W.J.
    Biochemical characterization of the major Sorghum grain peroxidase (2006), FEBS J., 273, 2293-2307.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.11.1.7 Ca2+-binding increases the protein conformational stability by raising the melting temperature from 67°C to 82°C Sorghum bicolor

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.7 Ca2+ SPC4 is activated by Ca2+. Ca2+-binding increases the protein conformational stability by raising the melting temperature from 67°C to 82°C Sorghum bicolor

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.1.7 32000
-
 gel filtration Sorghum bicolor
1.11.1.7 38000
-
 1 * 38000, SDS-PAGE Sorghum bicolor

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.7 Sorghum bicolor P84516 Moench var. Cauga 108–15
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.11.1.7 glycoprotein SPC4 consists of two glycoforms with molecular masses of 34227 Da and 35629 Da. Sugar contents of 3.0% w/w and 6.7% w/w in glycoform I and II, respectively, and a mass of the apoprotein of 33 246 Da. The glycosylation sites of SPC4 are localized in the C-terminus part of the enzyme. Main sugar constituents of the glycan chains are fucose, mannose, xylose, and N-acetylglucosamine Sorghum bicolor

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.7
-
 Sorghum bicolor

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.1.7 seed
-
 Sorghum bicolor
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.11.1.7 additional information
-
-
 Sorghum bicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.7 ferulic acid + H2O2
-
 Sorghum bicolor ?
-
 ?
1.11.1.7 indole-3-acetic acid + H2O2
-
 Sorghum bicolor ?
-
 ?
1.11.1.7 N-acetyl-L-tyrosine + H2O2
-
 Sorghum bicolor ?
-
 ?
1.11.1.7 N-acetyl-L-tyrosine methyl ester + H2O2
-
 Sorghum bicolor ?
-
 ?
1.11.1.7 p-coumaric acid + H2O2
-
 Sorghum bicolor ?
-
 ?
1.11.1.7 reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
-
 Sorghum bicolor oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.1.7 monomer 1 * 38000, SDS-PAGE Sorghum bicolor
1.11.1.7 monomer 1 * 34283–35631, MALDI-TOF-MS Sorghum bicolor

Synonyms

EC Number Synonyms Comment Organism
1.11.1.7 SPC4
-
 Sorghum bicolor

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.11.1.7 55
-
 in the absence of added CaCl2, SPC4 readily loses activity when incubated at temperatures above 55°C Sorghum bicolor
1.11.1.7 67
-
 Ca2+-binding increases the protein conformational stability by raising the melting temperature from 67°C to 82°C Sorghum bicolor
1.11.1.7 82
-
 Ca2+-binding increases the protein conformational stability by raising the melting temperature from 67°C to 82°C Sorghum bicolor

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.7 3.8
-
 reaction with reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) Sorghum bicolor
1.11.1.7 5.5
-
 reaction with ferulic acid Sorghum bicolor
1.11.1.7 6.5
-
 reaction with N-acetyl-L-tyrosine Sorghum bicolor

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.11.1.7 3 7 25°C, 2 h, stable Sorghum bicolor

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.7 heme the enzyme contains a type-b heme Sorghum bicolor

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.11.1.7 Sorghum bicolor calculated from sequence
-
 11