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Literature summary extracted from

  • Sheikh, I.A.; Singh, A.K.; Singh, N.; Sinha, M.; Singh, S.B.; Bhushan, A.; Kaur, P.; Srinivasan, A.; Sharma, S.; Singh, T.P.
    Structural evidence of substrate specificity in mammalian peroxidases: structure of the thiocyanate complex with lactoperoxidase and its interactions at 2.4 A resolution (2009), J. Biol. Chem., 284, 14849-14856.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.7 in complex with thiocyanate, hanging drop vapour diffusion method, using 0.2 M ammonium iodide and 20% (w/v) polyethylene glycol 3350 Bubalus bubalis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.1.7 thiocyanate + H2O2 Bubalus bubalis
-
?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.7 Bubalus bubalis
-
Murrah buffaloe
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.7 CM-Sephadex C-50 gel filtration and Sephadex G-100 gel filtration Bubalus bubalis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.1.7 milk
-
Bubalus bubalis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.7 reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
-
Bubalus bubalis oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
-
?
1.11.1.7 thiocyanate + H2O2
-
Bubalus bubalis ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.7 lactoperoxidase
-
Bubalus bubalis
1.11.1.7 LPO
-
Bubalus bubalis

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.7 heme
-
Bubalus bubalis