1.1.1.337: L-2-hydroxycarboxylate dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about L-2-hydroxycarboxylate dehydrogenase (NAD+), go to the full flat file.
Word Map on EC 1.1.1.337
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1.1.1.337
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lactobacillus
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confusus
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dehydrogenases
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l-lactate
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nadh-dependent
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jannaschii
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sulfite
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2-oxoisocaproate
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cysteate
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desulfonation
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dogfish
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methanogen
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methanocaldococcus
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synthesis
- 1.1.1.337
- lactobacillus
- confusus
- dehydrogenases
- l-lactate
-
nadh-dependent
- jannaschii
- sulfite
- 2-oxoisocaproate
- cysteate
-
desulfonation
-
dogfish
-
methanogen
- methanocaldococcus
- synthesis
Reaction
Synonyms
(R)-sulfolactate dehydrogenase, ComC, L-2-hydroxyacid dehydrogenase, L-2-hydroxyacid dehydrogenase (NAD+), L-2-hydroxyisocaproate dehydrogenase, L-HicDH, L-hydroxyisocaproate dehydrogenase, L-sulfolactate dehydrogenase, MDH I, MJ1425, sulfolactate dehydrogenase
ECTree
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Temperature Stability
Temperature Stability on EC 1.1.1.337 - L-2-hydroxycarboxylate dehydrogenase (NAD+)
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52
heat capacity function of the enzyme shows a single peak with the T(m) values between 52.14° C and 55.89°C at pH 7.0 at different scan rates
additional information
the thermal denaturation of the enzyme is studied by Differential Scanning Calorimetry and Circular Dichroism spectroscopy. The thermal denaturation is pH dependent. The thermal denaturation is irreversible and the T(m) is dependent on the scan-rate. Stabilizing effect of NADH binding. The denaturation process of L-HicDH is kinetically determined
additional information
-
the thermal denaturation of the enzyme is studied by Differential Scanning Calorimetry and Circular Dichroism spectroscopy. The thermal denaturation is pH dependent. The thermal denaturation is irreversible and the T(m) is dependent on the scan-rate. Stabilizing effect of NADH binding. The denaturation process of L-HicDH is kinetically determined