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Literature summary extracted from

  • Deshpande, A.R.; Wagenpfeil, K.; Pochapsky, T.C.; Petsko, G.A.; Ringe, D.
    Metal-dependent function of a mammalian acireductone dioxygenase (2016), Biochemistry, 55, 1398-1407 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.53 Ni- and Co-bound proteins. Both Ni and Co present an octahedral coordination geometry in the active site bound to protein ligands H88, H90, H133 and E94. Additionally, two distinct water (or hydroxide) ligands bind to the metal ion center Mus musculus
1.13.11.54 Ni- and Co-bound proteins. Both Ni and Co present an octahedral coordination geometry in the active site bound to protein ligands H88, H90, H133 and E94. Additionally, two distinct water (or hydroxide) ligands bind to the metal ion center Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.53 0.0493
-
(1Z)-1,2-dihydroxyhex-1-en-3-one Co2+ bound enzyme, pH 7.0, 25°C Mus musculus
1.13.11.53 0.2871
-
(1Z)-1,2-dihydroxyhex-1-en-3-one Ni2+ bound enzyme, pH 7.0, 25°C Mus musculus
1.13.11.54 0.1185
-
(1Z)-1,2-dihydroxyhex-1-en-3-one Fe2+ bound enzyme, pH 7.0, 25°C Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.53 Co2+ Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable Mus musculus
1.13.11.53 Fe2+ the Fe2+ bound protein catalyzes the reaction of EC 1.13.11.54 Mus musculus
1.13.11.53 Mn2+ Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable Mus musculus
1.13.11.53 additional information the identity of bound metal ion does not affect the oligomeric state of ARD Mus musculus
1.13.11.53 Ni2+ Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable Mus musculus
1.13.11.54 Co2+ the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53 Mus musculus
1.13.11.54 Fe2+ Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable Mus musculus
1.13.11.54 Mn2+ the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53 Mus musculus
1.13.11.54 additional information the identity of bound metal ion does not affect the oligomeric state of ARD Mus musculus
1.13.11.54 Ni2+ the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53 Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.11.53 23000 26000 gel filtration Mus musculus
1.13.11.54 23000 26000 gel filtration Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.53 Mus musculus
-
-
-
1.13.11.54 Mus musculus Q99JT9
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.53 (1Z)-1,2-dihydroxyhex-1-en-3-one + O2 i.e. desthio-acireductone Mus musculus n-butanoic acid + formic acid + CO
-
?
1.13.11.54 (1Z)-1,2-dihydroxyhex-1-en-3-one + O2 i.e. desthio-acireductone Mus musculus 2-oxovalerate + formic acid
-
?

Subunits

EC Number Subunits Comment Organism
1.13.11.53 monomer 1 * 21500, calculated Mus musculus
1.13.11.54 monomer 1 * 21500, calculated Mus musculus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.13.11.53 43
-
Mn2+ bound enzyme, melting temperature Mus musculus
1.13.11.53 58
-
Ni2+ bound enzyme, melting temperature Mus musculus
1.13.11.54 43
-
Mn2+ bound enzyme, melting temperature Mus musculus
1.13.11.54 58
-
Ni2+ bound enzyme, melting temperature Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.53 7.87
-
(1Z)-1,2-dihydroxyhex-1-en-3-one Co2+ bound enzyme, pH 7.0, 25°C Mus musculus
1.13.11.53 17.1
-
(1Z)-1,2-dihydroxyhex-1-en-3-one Ni2+ bound enzyme, pH 7.0, 25°C Mus musculus
1.13.11.54 111.7
-
(1Z)-1,2-dihydroxyhex-1-en-3-one Fe2+ bound enzyme, pH 7.0, 25°C Mus musculus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.13.11.53 60
-
(1Z)-1,2-dihydroxyhex-1-en-3-one Ni2+ bound enzyme, pH 7.0, 25°C Mus musculus
1.13.11.53 160
-
(1Z)-1,2-dihydroxyhex-1-en-3-one Co2+ bound enzyme, pH 7.0, 25°C Mus musculus
1.13.11.54 950
-
(1Z)-1,2-dihydroxyhex-1-en-3-one Fe2+ bound enzyme, pH 7.0, 25°C Mus musculus