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L5135

Sigma-Aldrich

L-Leucine Dehydrogenase from Bacillus cereus

lyophilized powder, ≥60 units/mg protein

Sinónimos:

L-Leucine:NAD+ oxidoreductase (deaminating)

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About This Item

Número de CAS:
9082-71-7
Comisión internacional de enzimas:
1.4.1.9 (BRENDA, IUBMB)
MDL number:
MFCD00147461
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

Quality Level

200

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.

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.

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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 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
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)
Emily P Balskus et al.
Journal of the American Chemical Society, 131(41), 14648-14649 (2009-09-29)
Previous studies of the biosynthetic enzymes involved in the assembly of scytonemin (1), a cyanobacterial sunscreen, have identified beta-ketoacid 2 as an important intermediate that is produced by ThDP-dependent enzyme ScyA. We now report that ScyC, previously annotated as a
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