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L5135

Sigma-Aldrich

L-Leucin-Dehydrogenase aus Bacillus cereus

lyophilized powder, ≥60 units/mg protein

Synonym(e):

L-Leucine:NAD+ oxidoreductase (deaminating)

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About This Item

CAS-Nummer:
9082-71-7
EC-Nummer:
1.4.1.9 (BRENDA, IUBMB)
MDL-Nummer:
MFCD00147461
UNSPSC-Code:
12352204
NACRES:
NA.54

Form

lyophilized powder

Qualitätsniveau

200

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.

Anwendung

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

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.

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)

Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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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)
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
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
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
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