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)
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)
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
N M Brunhuber et al.
The Journal of biological chemistry, 269(23), 16203-16211 (1994-06-10)
L-Phenylalanine dehydrogenase catalyzes the NAD(+)-dependent, reversible, oxidative deamination of L-phenylalanine to form ammonia, phenyl pyruvate, and NADH. The enzyme has been purified to homogeneity from Rhodococcus sp. M4, and a partial amino acid sequence was obtained. A cosmid library of
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