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Literature summary for 1.1.3.15 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
Search for more literature for 1.1.3.15

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

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

Localization

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

Organism

Organism UniProt Comment Textmining
Rattus sp.
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Storage Stability

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Cofactor

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

Ki Value [mM]

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