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Literature summary for 1.11.1.7 extracted from

  • Fielding, A.J.; Singh, R.; Boscolo, B.; Loewen, P.C.; Ghibaudi, E.M.; Ivancich, A.
    Intramolecular electron transfer versus substrate oxidation in lactoperoxidase: investigation of radical intermediates by stopped-flow absorption spectrophotometry and (9-285 GHz) electron paramagnetic resonance spectroscopy (2008), Biochemistry, 47, 9781-9792.
    View publication on PubMed
Search for more literature for 1.11.1.7

Organism

Organism UniProt Comment Textmining
Bos taurus P80025
-
-

Source Tissue

Source Tissue Comment Organism Textmining
milk
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzohydroxamic acid + H2O2 the estimated rate constant is approximately one-tenth of that of o-dianisidine Bos taurus ?
-
 ?
mitoxanthrone + H2O2
-
 Bos taurus ?
-
 ?
o-anisidine + H2O2 the peroxidase specific activities determined under comparable conditions (pH 8 and 5°C) reveal that of o-anisidine to be one-tenth of that of o-dianisidine Bos taurus ?
-
 ?
o-dianisidine + H2O2 best electron donor Bos taurus ?
-
 ?
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
-
 Bos taurus oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
-
 ?

Synonyms

Synonyms Comment Organism
lactoperoxidase
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 Bos taurus
LPO
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 Bos taurus

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 8 the specific activity of the enzyme is 600times higher at pH 5.0 than at pH 8.0 Bos taurus

Cofactor

Cofactor Comment Organism Structure
heme
-
 Bos taurus