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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
Hongmei Li et al.
Applied biochemistry and biotechnology, 158(2), 343-351 (2008-07-16)
Although an X-ray model sequence of a leucine dehydrogenase from Bacillus sphaericus ATCC4525 was reported, the amino acid sequence of this enzyme has not been confirmed. In the current study, this leucine dehydrogenase gene was cloned, sequenced, and over-expressed in
Peng-Hu Zhang et al.
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 23(2), 268-272 (2007-04-28)
The purification and the characteristics of an enzyme from Morganella morganii J-8, which could produce d-pseudoephedrine from 1-phenyl-2-methylamine-acetone, were performed in this study. In this research, first, cells were disrupted by ultrasonic treatment at 4 degrees C. The carbonyl enantioselective
M B Ansorge et al.
Biotechnology and bioengineering, 68(5), 557-562 (2000-05-08)
A method for the production of recombinant L-leucine dehydrogenase from Bacillus cereus in pilot scale is described employing the temperature induced runaway replication vector pIET98 and the Escherichia coli host strain BL21. Fed-batch cultivation using a semi-synthetic high-cell densitiy medium
Tatyana A Muranova et al.
Acta crystallographica. Section D, Biological crystallography, 58(Pt 6 Pt 2), 1059-1062 (2002-05-31)
Leucine dehydrogenase is an octameric enzyme which belongs to the superfamily of amino-acid dehydrogenases and catalyses the reversible oxidative deamination of leucine to 2-ketoisocaproate, with the corresponding reduction of the cofactor NAD(+). Catalysis by this enzyme is thought to involve
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