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Literature summary for 1.13.11.54 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)

Crystallization (Comment) Organism
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]

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

Metals/Ions

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23000 26000 gel filtration Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q99JT9
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
monomer 1 * 21500, calculated Mus musculus

Temperature Stability [°C]

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

Turnover Number [1/s]

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

kcat/KM [mM/s]

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