P4798
L-Phenylalanine Dehydrogenase from Sporosarcina sp.
lyophilized powder, ≥6 units/mg solid
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥6 units/mg solid
Biological source:
bacterial (Sporosarcina sp.)
Concentration:
≤100%
biological source
bacterial (Sporosarcina sp.)
Quality Level
form
lyophilized powder
specific activity
≥6 units/mg solid
storage condition
dry at room temperature
concentration
≤100%
color
white to light brown
application(s)
life science and biopharma
storage temp.
−20°C
General description
Research area: CELL SIGNALING
Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine ε-dehydrogenase, and meso-a,ε-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure.
Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine ε-dehydrogenase, and meso-a,ε-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure.
Biochem/physiol Actions
Phenylalanine dehydrogenase (PheDH) is considered an effective enzyme to estimate the quantity of phenylalanine to distinguish phenylketonuria (PKU) disease.Moreover, it is utilized for the production of optically pure l-phenylalanine, a key component of the artificial sweetener aspartame. L-Phenylalanine dehydrogenase is a NAD+-dependent oxidoreductase that catalyzes the reversible, oxidative deamination of L-phenylalanine, which results in its degradation. L-Phenylalanine dehydrogenase is used to study phenylalanine metabolism and phenylalanine, tyrosine, and tryptophan biosynthesis.
Other Notes
One unit will oxidize 1.0 μmole of L-phenylalanine per min at pH 10.5 at 30 °C in the presence of β-NAD.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Increase of Bacillus badius Phenylalanine dehydrogenase specificity towards phenylalanine substrate by site-directed mutagenesis
Yousefi F, et al.
Archives of Biochemistry and Biophysics, 635, 44-51 (2017)
N M Brunhuber et al.
Biochemistry, 39(31), 9174-9187 (2000-08-05)
Phenylalanine dehydrogenase catalyzes the reversible, pyridine nucleotide-dependent oxidative deamination of L-phenylalanine to form phenylpyruvate and ammonia. We have characterized the steady-state kinetic behavior of the enzyme from Rhodococcus sp. M4 and determined the X-ray crystal structures of the recombinant enzyme
N M Brunhuber et al.
The Journal of biological chemistry, 269(23), 16203-16211 (1994-06-10)
L-Phenylalanine dehydrogenase catalyzes the NAD(+)-dependent, reversible, oxidative deamination of L-phenylalanine to form ammonia, phenyl pyruvate, and NADH. The enzyme has been purified to homogeneity from Rhodococcus sp. M4, and a partial amino acid sequence was obtained. A cosmid library of
Enzymatic phenylalanine estimation for the management of patients with phenylketonuria.
U Wendel et al.
Clinica chimica acta; international journal of clinical chemistry, 201(1-2), 95-98 (1991-09-14)
J Tynan et al.
Protein expression and purification, 20(3), 421-434 (2000-11-23)
This study is concerned with further development of the kinetic locking-on strategy for bioaffinity purification of NAD(+)-dependent dehydrogenases. Specifically, the synthesis of highly substituted N(6)-linked immobilized NAD(+) derivatives is described using a rapid solid-phase modular approach. Other modifications of the
Global Trade Item Number
| SKU | GTIN |
|---|---|
| P4798-50UN | 04061832731162 |
| P4798-50MG | 04061832731155 |
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