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Literature summary extracted from

  • Kabine, M.; El Kebbaj, M.S.; Hafiani, A.; Latruffe, N.; Cherkaoui-Malki, M.
    Hibernation impact on the catalytic activities of the mitochondrial D-3-hydroxybutyrate dehydrogenase in liver and brain tissues of jerboa (Jaculus orientalis) (2003), BMC Biochem., 4, 11.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.30 additional information
-
 additional information dissociation constants for the cofactors and reaction kinetics at different physiological states in liver and brain Jaculus orientalis
1.1.1.30 0.058
-
 NADH euthermic state, brain Jaculus orientalis
1.1.1.30 0.074
-
 NADH euthermic state, liver Jaculus orientalis
1.1.1.30 0.146
-
 acetoacetate euthermic state, brain Jaculus orientalis
1.1.1.30 0.15
-
 acetoacetate euthermic state, liver Jaculus orientalis
1.1.1.30 0.238
-
 NAD+ euthermic state, liver Jaculus orientalis
1.1.1.30 0.633
-
 (R)-3-hydroxybutyrate euthermic state, liver Jaculus orientalis
1.1.1.30 1.187
-
 NAD+ euthermic state, brain Jaculus orientalis
1.1.1.30 2
-
 (R)-3-hydroxybutyrate euthermic state, brain Jaculus orientalis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.30 membrane
-
 Jaculus orientalis 16020
-
1.1.1.30 mitochondrion
-
 Jaculus orientalis 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.30 (R)-3-hydroxybutyrate + NAD+ Jaculus orientalis during hibernation, the enzyme is responsible for bioconvertion of high amounts of ketone bodies, i.e. acetoacetate and (R)-3-hydroxybutyrate, in the liver for usage as energetic fuel acetoacetate + NADH + H+
-
 r
1.1.1.30 additional information Jaculus orientalis enzyme activity is differently regulated in liver and brain at euthermic, prehibernating,and hibernating state ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.30 Jaculus orientalis
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.30 brain
-
 Jaculus orientalis
-
1.1.1.30 liver high activity Jaculus orientalis
-
1.1.1.30 additional information during the cold adaptation process, the prehibernating stage, the enzyme activity is decreased compared to euthermic state, in the hibernation state, the rate of acetoacetate reduction is increased in liver, while the oxidation of D-beta-hydroxybutyrate is increased in brain Jaculus orientalis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.30 (R)-3-hydroxybutyrate + NAD+
-
 Jaculus orientalis acetoacetate + NADH + H+
-
 r
1.1.1.30 (R)-3-hydroxybutyrate + NAD+ during hibernation, the enzyme is responsible for bioconvertion of high amounts of ketone bodies, i.e. acetoacetate and (R)-3-hydroxybutyrate, in the liver for usage as energetic fuel Jaculus orientalis acetoacetate + NADH + H+
-
 r
1.1.1.30 additional information enzyme activity is differently regulated in liver and brain at euthermic, prehibernating,and hibernating state Jaculus orientalis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.30 BDH
-
 Jaculus orientalis
1.1.1.30 D-beta-hydroxybutyrate dehydrogenase
-
 Jaculus orientalis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.30 37
-
 assay at Jaculus orientalis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.30 9 37
-
 Jaculus orientalis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.30 7.4
-
 assay at Jaculus orientalis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.30 NAD+
-
 Jaculus orientalis
1.1.1.30 NADH
-
 Jaculus orientalis