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Literature summary for 1.11.1.5 extracted from

  • Jasion, V.S.; Poulos, T.L.
    Leishmania major peroxidase is a cytochrome c peroxidase (2012), Biochemistry, 51, 2453-2460.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.5

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics, overview Leishmania major

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme is sensitive to increasing ionic strength Leishmania major

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ferrocytochrome c + H2O2 Leishmania major
-
 2 ferricytochrome c + 2 H2O
-
 ?
additional information Leishmania major Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities, but cytochrome c is the natural substrate ?
-
 ?

Organism

Organism UniProt Comment Textmining
Leishmania major
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2 ferrocytochrome c + H2O2 + 2 H+ = 2 ferricytochrome c + 2 H2O the intermediate Compound I forms once H2O2 is heterolytically cleaved, releasing a water molecule. The remaining O atom oxidizes the heme iron to Fe(IV) and an organic moiety to a cation radical. For most heme peroxidases, this moiety is the porphyrin ring. Upon two electron transfer events from two substrate molecules, the enzyme returns to the resting state with water occupying the active site Leishmania major
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferrocytochrome c + H2O2
-
 Leishmania major 2 ferricytochrome c + 2 H2O
-
 ?
additional information Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities, but cytochrome c is the natural substrate Leishmania major ?
-
 ?
additional information Leishmania major cytochrome c has an electropositive surface surrounding the exposed heme edge that serves as the docking site with redox partners. Kinetic assays performed with Leishmania major cytochrome c and the enzyme show that it is a much better substrate for LmP than horse heart cytochrome c Leishmania major ?
-
 ?

Synonyms

Synonyms Comment Organism
CCP
-
 Leishmania major
cytochrome c peroxidase
-
 Leishmania major
LmP
-
 Leishmania major

General Information

General Information Comment Organism
additional information enzyme-cytochrome c protein-protein docking and modeling, overview Leishmania major