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Enzymes for Research, Diagnostic and Industrial Use

Leucine dehydrogenase from Microorganism

Cat No.
NATE-1715
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
LEDH (Microorganism)
Source
Microorganism
Form
White powder, lyophilized
Enzyme Commission Number
EC 1.4.1.9
Activity
>500U/mg protein
CAS No.
9082-71-7
Molecular Weight
43 kDa (SDS-PAGE)
Isoelectric point
6.6
pH Stability
6.0~11.0 (25℃, 15hr)
Michaelis Constant
2.6×10^-4 M (NAD )
2.0×10^-3 M(L-Leucine)
6.8×10^-4 M(α-Ketoisocaproate)
4.2×10^-2 M (NH Cl)
2.3×10^-4 M (NADH)
Unit Definition
One unit will convert one micromole of L-Leucine to α-Ketoisocaproate per minute at pH 10.5 at 37℃.
Optimum pH
above11.0(L-Leu→α-K I C),
8.5(α-K I C→L-Leu)
Optimum temperature
55-60℃(L-Leu →α-K I C)
above 60℃(α-K I C→L-Leu)
Thermal stability
< 55℃(pH 7.0, 20min)
Storage
Store at -20°C.
Inhibitors
Hg2+
Synonyms
EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH
Notes
INTENDED FOR RESEARCH USE ONLY, NOT FOR USE IN HUMAN, THERAPEUTIC OR DIAGNOSTIC APPLICATIONS.
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Related Protocols
leucine dehydrogenase -Enzymatic Assay Protocol
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