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Literature summary extracted from

  • Belmouden, A.; Lederer, F.
    The role of a beta barrel loop 4 extension in modulating the physical and functional properties of long-chain 2-hydroxy-acid oxidase isozymes (1996), Eur. J. Biochem., 238, 790-798.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.15 expression in Escherichia coli Rattus sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.15 oxalate competitive inhibition Rattus sp.
1.1.3.15 pyruvate competitive inhibition Rattus sp.
1.1.3.15 trans-cinnamate competitive inhibition Rattus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.15 0.09
-
 L-Phenyllactate isozyme beta1 Rattus sp.
1.1.3.15 0.13
-
 L-Phenyllactate isozyme beta2 Rattus sp.
1.1.3.15 0.16
-
 L-Mandelate isozyme beta1 Rattus sp.
1.1.3.15 0.23
-
 L-Mandelate isozyme beta2 Rattus sp.
1.1.3.15 0.3
-
 L-2-Hydroxyisocaproate isozyme beta1 Rattus sp.
1.1.3.15 0.32
-
 L-2-Hydroxyisocaproate isozyme beta2 Rattus sp.
1.1.3.15 0.7
-
 DL-2-hydroxy-4-methylthiobutanoic acid
-
 Rattus sp.
1.1.3.15 1.1
-
 DL-2-hydroxy-4-methylthiobutanoic acid isozyme beta2 Rattus sp.
1.1.3.15 2.04
-
 DL-2-hydroxybutyrate isozyme beta2 Rattus sp.
1.1.3.15 2.5
-
 DL-2-hydroxybutyrate isozyme beta1 Rattus sp.
1.1.3.15 4.7
-
 L-lactate isozyme beta2 Rattus sp.
1.1.3.15 5.3
-
 L-leucine isozyme beta2 Rattus sp.
1.1.3.15 6.1
-
 L-lactate isozyme beta1 Rattus sp.
1.1.3.15 6.4
-
 L-leucine isozyme beta1 Rattus sp.

Localization

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.15 Rattus sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.15 recombinant isozymes beta1, beta2 Rattus sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.3.15 0.78
-
 isozyme beta1 Rattus sp.

Storage Stability

EC Number Storage Stability Organism
1.1.3.15 4°C, 60% ammonium sulfate precipitate, several months Rattus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.15 DL-2-hydroxy-4-methylthiobutanoic acid + 2,6-dichlorophenolindophenol
-
 Rattus sp. 2-oxo-4-methylthiobutanoic acid + reduced 2,6-dichlorophenolindophenol
-
 ?
1.1.3.15 DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
-
 Rattus sp. 2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
-
 ?
1.1.3.15 L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol
-
 Rattus sp. 2-oxoisocaproate + reduced 2,6-dichlorophenolindophenol
-
 ?
1.1.3.15 L-lactate + 2,6-dichlorophenolindophenol
-
 Rattus sp. pyruvate + reduced 2,6-dichlorophenolindophenol
-
 ?
1.1.3.15 L-leucine + 2,6-dichlorophenolindophenol
-
 Rattus sp. ? + reduced 2,6-dichlorophenolindophenol
-
 ?
1.1.3.15 L-mandelate + 2,6-dichlorophenolindophenol
-
 Rattus sp. oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
 ?
1.1.3.15 L-phenyllactate + 2,6-dichlorophenolindophenol
-
 Rattus sp. phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.15 0.014
-
 L-leucine isozymes beta1 and beta2 Rattus sp.
1.1.3.15 0.26
-
 L-lactate isozyme beta1 Rattus sp.
1.1.3.15 0.38
-
 L-lactate isozyme beta2 Rattus sp.
1.1.3.15 0.59
-
 L-Phenyllactate isozyme beta1 Rattus sp.
1.1.3.15 0.7
-
 L-Phenyllactate isozyme beta2 Rattus sp.
1.1.3.15 1.55
-
 L-Mandelate isozyme beta1 Rattus sp.
1.1.3.15 1.66
-
 DL-2-hydroxybutyrate isozyme beta1 Rattus sp.
1.1.3.15 1.9
-
 DL-2-hydroxy-4-methylthiobutanoic acid isozyme beta2 Rattus sp.
1.1.3.15 2
-
 L-2-Hydroxyisocaproate isozyme beta1 Rattus sp.
1.1.3.15 2
-
 DL-2-hydroxybutyrate isozyme beta2 Rattus sp.
1.1.3.15 2.1
-
 DL-2-hydroxy-4-methylthiobutanoic acid isozyme beta1 Rattus sp.
1.1.3.15 2.4
-
 L-2-Hydroxyisocaproate isozyme beta2 Rattus sp.
1.1.3.15 2.51
-
 L-Mandelate isozyme beta2 Rattus sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.15 FMN three-residue insertion of loop 4 in isozyme beta2 influences ionisation state of FMN Rattus sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.3.15 1
-
 trans-cinnamate isozyme beta1 Rattus sp.
1.1.3.15 1.9
-
 trans-cinnamate isozyme beta2 Rattus sp.
1.1.3.15 10.5
-
 oxalate isozyme beta1 Rattus sp.
1.1.3.15 15.9
-
 pyruvate isozyme beta1 Rattus sp.
1.1.3.15 18.3
-
 pyruvate isozyme beta2 Rattus sp.
1.1.3.15 23
-
 oxalate isozyme beta2 Rattus sp.