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Literature summary extracted from

  • Cunane, L.M.; Barton, J.D.; Chen, Z.W.; Le, K.H.; Amar, D.; Lederer, F.; Mathews, F.S.
    Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase (2005), Biochemistry, 44, 1521-1531.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.3.15 sitting drop vapor diffusion method, 0.005 ml of protein solution containing 10 mg/ml protein in 0.1 M Tris, pH 7.5, mixed with the same volume of reservoir solution containing 0.4 M sodium acetate and 0.2 M sodium citrate, pH 6.5, equilibration at 4°C, soaking of crystals in 25% glycerol-containing reservoir solution, X-ray diffraction structure determination and analysis at 2.3 A resolution Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.15 additional information
-
 additional information steady-state kinetics Rattus norvegicus
1.1.3.15 0.046
-
 L-2-hydroxy octanoate
-
 Rattus norvegicus
1.1.3.15 1.36
-
 L-2-hydroxy palmitate
-
 Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.3.15 peroxisome
-
 Rattus norvegicus 5777
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.15 Rattus norvegicus Q07523
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.3.15 an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2 the catalytic residue is Phe23, reaction mechanism Rattus norvegicus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.3.15 kidney
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.15 L-2-hydroxy octanoate + O2
-
 Rattus norvegicus 2-oxo-octanoate + H2O2
-
 ?
1.1.3.15 L-2-hydroxy palmitate + O2
-
 Rattus norvegicus 2-oxo-palmitate + H2O2
-
 ?
1.1.3.15 L-lactate + O2
-
 Rattus norvegicus pyruvate + H2O2
-
 ?
1.1.3.15 mandelate + O2 oxidation of an L-2-hydroxy acid to a 2-oxoacid, model for the binding of L-mandelate into the active site, overview Rattus norvegicus phenylpyruvate + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.3.15 More structure analysis, modelling, the enzyme shows the same beta8alpha8 TIM barrel structure as other structurally characterized family members of the FMN-dependent enzyme family Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
1.1.3.15 LCHAO
-
 Rattus norvegicus
1.1.3.15 long chain hydroxy acid oxidase
-
 Rattus norvegicus
1.1.3.15 More the enzyme belongs to the FMN-dependent enzyme family Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.15 0.34
-
 L-2-hydroxy palmitate
-
 Rattus norvegicus
1.1.3.15 0.99
-
 L-2-hydroxy octanoate
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.15 FMN dependent on Rattus norvegicus