L5135
L-Leucine Dehydrogenase from Bacillus cereus
lyophilized powder, ≥60 units/mg protein
Synonym(s):
L-Leucine:NAD+ oxidoreductase (deaminating)
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Pricing and availability is not currently available.
Recommended Products
form
lyophilized powder
Quality Level
specific activity
≥60 units/mg protein
mol wt
245 kDa
storage temp.
−20°C
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General description
L-Leucine Dehydrogenase is a member of the amino acid dehydrogenase family.[1]
Application
L-Leucine Dehydrogenase from Bacillus cereus has been used to determine the branched-chain amino acids (BCAA) spectrophotometrically in serum samples.[2]
Biochem/physiol Actions
Leucine Dehydrogenase is a nicotinamide adenine dinucleotide hydrogen (NADH)-dependent oxidoreductase. It is involved in catalyzing the reductive amination of aliphatic 2-oxo-acids to their respective L-amino acids.[3]
Unit Definition
One unit will convert 1.0 μmole of L‑leucine to α-ketoisocaproate per min at pH 10.5 at 37 °C.
Other Notes
contains lysine
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Junping Zhou et al.
Biotechnology journal, 14(3), e1800253-e1800253 (2018-07-28)
Unnatural amino acids (UAAs) play a key role in modern medicinal chemistry such as small molecules and peptide-based drugs with fast-growing markets. Low efficiency for natural enzymes including leucine dehydrogenase (LeuDH, EC1.4.1.9) are one major challenge for UAA production. Here
N Kiba et al.
Journal of chromatography. A, 724(1-2), 355-357 (1996-02-16)
A liquid chromatographic system with a co-immobilized leucine dehydrogenase-NADH oxidase reactor is described for the determination of branched-chain amino acids such as I-leucine, I-isoleucine and I-valine. The enzymes were simultaneously immobilized on tresylate-containing poly(vinyl alcohol) beads. The separation was achieved
T Oikawa et al.
Biochemical and biophysical research communications, 280(4), 1177-1182 (2001-02-13)
X-ray crystallographic studies revealed that various amino acid dehydrogenases fold into two domains in each subunit, a substrate-binding domain and an NAD(P)(+)-binding domain (Baker, P. J., Turnbull, A. P., Sedelnikova, S. E., Stillman, T. J., and Rice, D. W. (1995)
P R Beckett et al.
Analytical biochemistry, 240(1), 48-53 (1996-08-15)
Plasma amino acid concentrations fall during insulin infusion. Amino acid concentrations can be maintained using an infusion of amino acids if their plasma concentration can be determined within a few minutes. We developed a spectrophometric assay which determines the total
A Sutherland et al.
Bioorganic & medicinal chemistry letters, 9(14), 1941-1944 (1999-08-18)
A series of novel 3-substituted 2-oxobutanoic acids were prepared and incubated with leucine dehydrogenase giving in one case both a kinetic resolution at C-3 and reductive amination of the ketone. This is the first example of an amino acid dehydrogenase
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