The enzyme from the archaeon Methanocaldococcus jannaschii catalyses the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates) . The enzyme can use both NADH and NADPH, although activity is higher with NADPH [1-3]. The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP+ . The same organism also possesses an NAD+-specific enzyme with similar activity, cf. EC 1.1.1.337, L-2-hydroxycarboxylate dehydrogenase (NAD+).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(2S)-2-hydroxycarboxylate:NAD(P)+ oxidoreductase
The enzyme from the archaeon Methanocaldococcus jannaschii catalyses the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates) [1]. The enzyme can use both NADH and NADPH, although activity is higher with NADPH [1-3]. The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP+ [1]. The same organism also possesses an NAD+-specific enzyme with similar activity, cf. EC 1.1.1.337, L-2-hydroxycarboxylate dehydrogenase (NAD+).
Vmax/KM: 120 /min*mg. The enzyme prefers oxaloacetate over 3-sulfopyruvate using NADH as cofactor. The enzyme prefers NADPH over NADH in reduction of oxaloacetate
Vmax/KM: 120 /min*mg. The enzyme prefers oxaloacetate over 3-sulfopyruvate using NADH as cofactor. The enzyme prefers NADPH over NADH in reduction of oxaloacetate
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
preference of NADP(H) over NAD(H). The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases
preference of NADP(H) over NAD(H).. The ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C. The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases
preference of NADP(H) over NAD(H). The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases
preference of NADP(H) over NAD(H). The ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C. The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases
in the presence of NADPH, 10 mM MgCl2, MnCl2 or CaCl2 is required to support full activity. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration
in the presence of NADPH, full enzymatic activity requires a minimum salt concentration of 0.1 M NaCl or KCl. At lower salt concentrations, the activity decreases by a factor of three. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration
in the presence of NADPH, 10 mM MgCl2, MnCl2 or CaCl2 is required to support full activity. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration
in the presence of NADPH, 10 mM MgCl2, MnCl2 or CaCl2 is required to support full activity. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration
in the presence of NADPH, full enzymatic activity requires a minimum salt concentration of 0.1 M NaCl or KCl. At lower salt concentrations, the activity decreases by a factor of three. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration
enzymatic activity of the dimeric enzyme is controlled by a pH-dependent transition between an active and inactive dimeric state at pH 7 without dissociation of the subunits
the effects of high temperature, cofactor binding, and high phosphate concentration are studied. They do not modify the oligomeric state of the enzyme. Enzymatic activity of the dimeric enzyme is controlled by a pH-dependent transition at pH 7 without dissociation of the subunits
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
determined in two crystal forms: a dimeric structure in the orthorhombic crystal at 1.9 A resolution and a tetrameric structure in the tetragonal crystal at 2.8 A
the three-dimensional structure is determined in two crystal forms: a dimeric structure in the orthorhombic crystal at 1.9 A resolution and a structure in the tetragonal crystal at 2.8 A
the three-dimensional structure of its gene product has been determined in two crystal forms: a dimeric structure in the orthorhombic crystal at 1.9 A resolution and a tetrameric structure in the tetragonal crystal at 2.8 A
Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases