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
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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 as an effective enzyme to estimate the quantity of phenylalanine to distinguish phenylketonuria (PKU) disease.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.
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Danger
hcodes
pcodes
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)
Y Asano et al.
European journal of biochemistry, 168(1), 153-159 (1987-10-01)
Phenylalanine dehydrogenase produced by Bacillus badius IAM 11059 was purified from the crude extract of B. badius to homogeneity, as judged by disc gel electrophoresis. The enzyme has an isoelectric point of 3.5 and a relative molecular mass, Mr, of
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
A Pasquo et al.
Acta crystallographica. Section D, Biological crystallography, 54(Pt 2), 269-272 (1998-10-08)
The NAD+-dependent phenylalanine dehydrogenase from Nocardia sp239 has been crystallized by the hanging-drop method of vapour diffusion using ammonium sulfate as the precipitant. Two crystal forms were obtained in the presence and absence of the enzyme substrates phenylpyruvic acid or
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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