추천 제품
생물학적 소스
bacterial (Sporosarcina sp.)
Quality Level
양식
lyophilized powder
특이 활성도
≥6 units/mg solid
저장 조건
dry at room temperature
농도
≤100%
색상
white to light brown
응용 분야
life science and biopharma
저장 온도
−20°C
일반 설명
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.
생화학적/생리학적 작용
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.
단위 정의
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.
신호어
Danger
유해 및 위험 성명서
예방조치 성명서
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
이미 열람한 고객
Rhodococcus-Phenylalanine Dehydrogenase:? Kinetics, Mechanism, and Structural Basis for Catalytic Specifity
Brunhuber NMW, et al.
Biochemistry, 38(31), 9174?9187-9174?9187 (2000)
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
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
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