Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Bode, R.; Birnbaum, D.
    Some properties of the leucine-biosynthesizing enzymes from Candida maltosa (1991), J. Basic Microbiol., 31, 21-26.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.3.13 Cd2+
-
Candida maltosa
2.3.3.13 Cu2+
-
Candida maltosa
2.3.3.13 Hg2+
-
Candida maltosa
2.3.3.13 K+ at high concentrations, stimulation at lower concentrations Candida maltosa
2.3.3.13 leucine competitive with respect to 2-oxo-3-methylbutanoate, non-competitive with respect to acetyl-CoA Candida maltosa
2.3.3.13 Zn2+
-
Candida maltosa
4.2.1.33 Cd2+ complete inhibition at 1 mM Candida maltosa
4.2.1.33 Co2+ 3% inhibition at 1 mM Candida maltosa
4.2.1.33 Cu2+ complete inhibition at 1 mM Candida maltosa
4.2.1.33 Fe2+ 13% inhibition at 1 mM Candida maltosa
4.2.1.33 Hg2+ complete inhibition at 1 mM Candida maltosa
4.2.1.33 Mg2+ 26% inhibition at 1 mM Candida maltosa
4.2.1.33 Mn2+ 45% inhibition at 1 mM Candida maltosa
4.2.1.33 Zn2+ complete inhibition at 1 mM Candida maltosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.3.13 additional information
-
additional information
-
Candida maltosa
2.3.3.13 0.064
-
acetyl-CoA
-
Candida maltosa
2.3.3.13 0.57
-
2-oxo-3-methylbutanoate
-
Candida maltosa
4.2.1.33 0.75
-
beta-carboxy-beta-hydroxyisocaproate
-
Candida maltosa
4.2.1.33 1.79
-
citraconate crude enzyme preparation Candida maltosa
4.2.1.33 4.57
-
alpha-hydroxy-beta-carboxyisocaproate
-
Candida maltosa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.3.13 K+ strongly dependent on the presence of monovalent cations, K+ is most effective Candida maltosa
2.3.3.13 K+ Km: 80 mM, inhibitory at higher concentrations Candida maltosa
2.3.3.13 Li+ can partially replace K+ in activation Candida maltosa
2.3.3.13 Rb+ can partially replace Rb+ in activation Candida maltosa
4.2.1.33 additional information no requirement Candida maltosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.3.13 2-oxo-3-methylbutanoate + acetyl-CoA + H2O Candida maltosa
-
?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.3.13 Candida maltosa
-
-
-
4.2.1.33 Candida maltosa
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.33 additional information
-
enzyme activity with citraconate 4.8-fold and 7.4-fold higher than with standard substrates Candida maltosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.3.13 2-oxo-3-methylbutanoate + acetyl-CoA + H2O
-
Candida maltosa 3-hydroxy-4-methyl-3-carboxypentanoate + CoA
-
?
2.3.3.13 2-oxo-3-methylbutanoate + acetyl-CoA + H2O
-
Candida maltosa ?
-
?
2.3.3.13 2-oxo-butanoate + acetyl-CoA + H2O
-
Candida maltosa 2-ethyl-2-hydroxysuccinic acid + CoA
-
?
2.3.3.13 pyruvate + acetyl-CoA + H2O
-
Candida maltosa 2-hydroxy-2-methylsuccinic acid + CoA
-
?
4.2.1.33 alpha-hydroxy-beta-carboxyisocaproate
-
Candida maltosa ?
-
?
4.2.1.33 beta-carboxy-beta-hydroxyisocaproate
-
Candida maltosa ?
-
?
4.2.1.33 citraconate
-
Candida maltosa ?
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.3.13 7.5 8.8
-
Candida maltosa
4.2.1.33 8.5
-
enzyme assay at Candida maltosa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.3.13 0.81
-
leucine competitive, with respect to 2-oxo-3-methylbutanoate Candida maltosa
2.3.3.13 1.3
-
leucine non-competitive, with respect to acetyl-CoA Candida maltosa
2.3.3.13 230
-
K+ at high concentration Candida maltosa