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Documentos Principais

L5135

Sigma-Aldrich

L-Leucine Dehydrogenase from Bacillus cereus

lyophilized powder, ≥60 units/mg protein

Sinônimo(s):

L-Leucine:NAD+ oxidoreductase (deaminating)

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About This Item

Número CAS:
Número da licença da enzima:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

forma

lyophilized powder

Nível de qualidade

atividade específica

≥60 units/mg protein

peso molecular

245 kDa

temperatura de armazenamento

−20°C

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Descrição geral

L-Leucine Dehydrogenase is a member of the amino acid dehydrogenase family.

Aplicação

L-Leucine Dehydrogenase from Bacillus cereus has been used to determine the branched-chain amino acids (BCAA) spectrophotometrically in serum samples.

Ações bioquímicas/fisiológicas

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.

Definição da unidade

One unit will convert 1.0 μmole of L‑leucine to α-ketoisocaproate per min at pH 10.5 at 37 °C.

Outras notas

contains lysine

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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K Selber et al.
Journal of chromatography. B, Biomedical sciences and applications, 743(1-2), 21-30 (2000-08-15)
Mathematical strategies were applied to optimise the extraction of recombinant leucine dehydrogenase from E. coli homogenates and endoglucanase 1 from culture filtrates of Trichoderma reesei in polyethylene glycol-phosphate systems. The goal was to test mathematical tools which could facilitate the
M B Ansorge et al.
Applied microbiology and biotechnology, 53(6), 668-673 (2000-08-05)
The established Escherichia coli expression vectors ptrc99a, pKK223-3, pPLlambda, pAsk75, pRA95, and pRA96, which differ in copy number, mode of induction, selection marker, and use of par sequences for stabilization, were investigated for the stable expression of recombinant L-leucine dehydrogenase
S Guangdong et al.
The Journal of antibiotics, 54(1), 66-73 (2001-03-28)
Shengjimycin is a group of 4"-acylated spiramycins with 4"-isovalerylspiramycin as the major component, produced by recombinant S. spiramyceticus F21 harboring a 4"-O-acyltransferase gene from S. mycarofaciens 1748. A stable bioengineered strain of Streptomyces spiramyceticus WSJ-1 was constructed by integrating the
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
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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