L5135
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:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
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Formulario
lyophilized powder
Nivel de calidad
actividad específica
≥60 units/mg protein
mol peso
245 kDa
temp. de almacenamiento
−20°C
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Descripción general
L-Leucine Dehydrogenase is a member of the amino acid dehydrogenase family.[1]
Aplicación
L-Leucine Dehydrogenase from Bacillus cereus has been used to determine the branched-chain amino acids (BCAA) spectrophotometrically in serum samples.[2]
Acciones bioquímicas o 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.[3]
Definición de unidad
One unit will convert 1.0 μmole of L‑leucine to α-ketoisocaproate per min at pH 10.5 at 37 °C.
Otras notas
contains lysine
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
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
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
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
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)
Julie Baussand et al.
PLoS computational biology, 5(9), e1000488-e1000488 (2009-09-05)
Communication between distant sites often defines the biological role of a protein: amino acid long-range interactions are as important in binding specificity, allosteric regulation and conformational change as residues directly contacting the substrate. The maintaining of functional and structural coupling
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