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Literature summary for 1.11.1.6 extracted from

  • Purwar, N.; McGarry, J.M.; Kostera, J.; Pacheco, A.A.; Schmidt, M.
    Interaction of nitric oxide with catalase: structural and kinetic analysis (2011), Biochemistry, 50, 4491-4503.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
fee enzyme and enzyme complexed with ammonia or NO, hanging drop vapor diffusion method, mixing of 0.004 ml of 12-13 mg/ml protein, containing NH4OH, with an equal volume of the reservoir solution consisting of 45-60 mM magnesium formate, pH 6.7, 2-3 weeks, soaking of crystals in ligand solutions, X-ray diffraction structure determination and analysis at 1.88-1.99 A resolution Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
NO generated from 1-(N,N-diethylamino)diazen-1-ium-1,2-diolate, competitive inhibitor, nitrosylated catalase is kinetically labile, NO tends to dissociate rapidly from the active site, binding structure, overview. Kinetic analysis of dissociation of NO from the enzyme-inhibitor complex Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
4 * 60000, SDS-PAGE Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 H2O2 Bos taurus
-
O2 + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus P00432
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 H2O2
-
Bos taurus O2 + 2 H2O
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 60000, SDS-PAGE Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Bos taurus