P4798
L-Phenylalanine Dehydrogenase from Sporosarcina sp.
lyophilized powder, ≥6 units/mg solid
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
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 €-dehydrogenase, and meso-a,€-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 €-dehydrogenase, and meso-a,€-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.
Unit Definition
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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)
Rhodococcus-Phenylalanine Dehydrogenase:? Kinetics, Mechanism, and Structural Basis for Catalytic Specifity
Brunhuber NMW, et al.
Biochemistry, 38(31), 9174?9187-9174?9187 (2000)
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
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)
Y Asano et al.
The Journal of biological chemistry, 262(21), 10346-10354 (1987-07-25)
NAD+-dependent phenylalanine dehydrogenases were purified 1,500- and 1,600-fold, and crystallized from Sporosarcina ureae SCRC-R04 and Bacillus sphaericus SCRC-R79a, respectively. The purified enzymes were homogeneous as judged by disc gel electrophoresis. The enzyme from S. ureae has a molecular weight of
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