P4798
L -苯丙氨酸脱氢酶 来源于芽孢八叠球菌 属
lyophilized powder, ≥6 units/mg solid
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥6 units/mg solid
Biological source:
bacterial (Sporosarcina sp.)
Concentration:
≤100%
biological source
bacterial (Sporosarcina sp.)
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
Quality Level
General description
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。
Biochem/physiol Actions
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。
Other Notes
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。
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
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)
Rhodococcus-Phenylalanine Dehydrogenase:? Kinetics, Mechanism, and Structural Basis for Catalytic Specifity
Brunhuber NMW, et al.
Biochemistry, 38(31), 9174?9187-9174?9187 (2000)
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.
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
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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