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:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥60 units/mg protein
form
lyophilized powder
specific activity
≥60 units/mg protein
mol wt
245 kDa
storage temp.
−20°C
Quality Level
General description
L-Leucine Dehydrogenase is a member of the amino acid dehydrogenase family.
Application
L-Leucine Dehydrogenase from Bacillus cereus has been used to determine the branched-chain amino acids (BCAA) spectrophotometrically in serum samples.
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.
Other Notes
One unit will convert 1.0 μmole of L‑leucine to α-ketoisocaproate per min at pH 10.5 at 37 °C.
contains lysine
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
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)
T Stoyan et al.
Journal of biotechnology, 54(1), 77-80 (1997-04-04)
The L-leucine dehydrogenase gene from Bacillus cereus (DSM 626) was cloned from a partial genomic library and sequenced. The open reading frame has 1101 bp and codes for a protein of 39.9 kDa. The deduced amino acid sequence of the
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
Stéphanie Chevalier et al.
Metabolism: clinical and experimental, 53(3), 388-396 (2004-03-12)
We propose that hyperinsulinemia stimulates protein synthesis when postabsorptive plasma amino acid (AA) concentrations are maintained. During a euglycemic hyperinsulinemic clamp, many AA, notably the branched-chain amino acids (BCAA), decline markedly. Therefore, we tested whether individual plasma AA could be
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