推荐产品
生物源
bacterial (Sporosarcina sp.)
品質等級
形狀
lyophilized powder
比活性
≥6 units/mg solid
儲存條件
dry at room temperature
濃度
≤100%
顏色
white to light brown
應用
life science and biopharma
儲存溫度
−20°C
一般說明
研究领域：细胞信号传导
苯丙氨酸脱氢酶是氨基酸脱氢酶大家族的成员，其包括谷氨酸脱氢酶、丙氨酸脱氢酶、亮氨酸脱氢酶、赖氨酸€-脱氢酶和内消旋-a,€-二氨基庚二酸D-脱氢酶。 有文献测过三种不同来源酶的基因序列。本品（来自脲芽孢八叠球菌）为八聚体。 具有双结构域的三维结构。
苯丙氨酸脱氢酶是氨基酸脱氢酶大家族的成员，其包括谷氨酸脱氢酶、丙氨酸脱氢酶、亮氨酸脱氢酶、赖氨酸€-脱氢酶和内消旋-a,€-二氨基庚二酸D-脱氢酶。 有文献测过三种不同来源酶的基因序列。本品（来自脲芽孢八叠球菌）为八聚体。 具有双结构域的三维结构。
生化／生理作用
苯丙氨酸脱氢酶(PheDH)可有效测定苯丙氨酸含量，用于分辨苯丙酮尿症(PKU)。L-苯丙氨酸脱氢酶是一种NAD+依赖性氧化还原酶，催化L-苯丙氨酸可逆性氧化脱氨，导致其降解。 L-苯丙氨酸脱氢酶用于研究苯丙氨酸代谢及苯丙氨酸、酪氨酸和色氨酸的生物合成。
單位定義
在 β-NAD 存在下，一个单位在 pH 10.5、30 ℃下每分钟氧化1.0 μ 摩尔的L-苯丙氨酸。
訊號詞
Danger
危險聲明
危險分類
Resp. Sens. 1
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 1
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, type N95 (US)
其他客户在看
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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