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P4798

Sigma-Aldrich

L-Phenylalanine Dehydrogenase from Sporosarcina sp.

lyophilized powder, ≥6 units/mg solid

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

Číslo CAS:
Číslo enzymu podle klasifikace EK:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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.

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.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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)
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
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
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

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