生物来源
bacterial (Sporosarcina sp.)
质量水平
表单
lyophilized powder
比活
≥6 units/mg solid
储存条件
dry at room temperature
浓度
≤100%
颜色
white to light brown
应用
life science and biopharma
储存温度
−20°C
一般描述
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）被认为是一种有效的酶，可用于估算苯丙氨酸数量以区分苯丙酮尿症（PKU）。此外，它还被用于生产光学纯l-苯丙氨酸，而l-苯丙氨酸是人工甜味剂阿斯巴甜的主要成分。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。
其他说明
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。
警示用语：
Danger
危险声明
预防措施声明
危险分类
Resp. Sens. 1
储存分类代码
11 - Combustible Solids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
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
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)
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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