Cat No.
DIA-209
Description
In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ ? 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis.
Abbr
Leucine dehydrogenase (Bacillus sp.)
Species
Bacillus sp.
Enzyme Commission Number
EC 1.4.1.9
Bio-activity
GradeⅡ 20U/mg-solid or more (containing approx. 70% of stabilizers)
Appearance
White amorphous powder, lyophilized
Molecular Mass
245 kDa
pH Stability
pH 5.5-10.5 (25°C, 20hr)
Michaelis Constant
1.0×10?3M (L-Leucine), 3.9×10??M (NAD?), 3.5×10??M (NADH), 3.1×10??M [α-Ketoisocaproate (α-KIC)], 2.0×10?1M (NH?)
Structure
6 subunits per mol of enzyme
Optimum pH
10.5-10.8 (L-Leu→α-KIC), 9.4 (α-KIC→L-Leu)
Optimum temperature
above 70°C
Stabilizers
2-Mercaptoethanol, L-cysteine, dithiothreitol, ethylenediaminetetraacetate
Thermal stability
below 60°C (pH 6.9, 10min)
Stability
Stable at-20°C for at least one year
Inhibitors
Na?S, Hg??, Cu??, Co??, Mg??, p-chloromercuribenzoate
Applications
This enzyme is useful for enzyme determination of L-leucine and the activity of leucine amino-peptidase.
Synonyms
EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH
