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L-Leucin-Dehydrogenase aus Bacillus cereus
lyophilized powder, ≥60 units/mg protein
Synonym(e):
L-Leucine:NAD+ oxidoreductase (deaminating)
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25 UNITS
CHF 863.00
CHF 863.00
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25 UNITS
CHF 863.00
About This Item
CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54
CHF 863.00
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Empfohlene Produkte
Form
lyophilized powder
Qualitätsniveau
Spezifische Aktivität
≥60 units/mg protein
Mol-Gew.
245 kDa
Lagertemp.
−20°C
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Allgemeine Beschreibung
L-Leucine Dehydrogenase is a member of the amino acid dehydrogenase family.[1]
Anwendung
L-Leucine Dehydrogenase from Bacillus cereus has been used to determine the branched-chain amino acids (BCAA) spectrophotometrically in serum samples.[2]
Biochem./physiol. Wirkung
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]
Einheitendefinition
One unit will convert 1.0 μmole of L‑leucine to α-ketoisocaproate per min at pH 10.5 at 37 °C.
Sonstige Hinweise
contains lysine
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
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
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
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
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
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