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Merck
CN

F4646

p-Fluoro-L-phenylalanine

别名:

4-Fluoro-L-phenylalanine

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经验公式(希尔记法):
C9H10FNO2
化学文摘社编号:
分子量:
183.18
PubChem Substance ID:
UNSPSC Code:
12352200
Beilstein/REAXYS Number:
2416148
MDL number:
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SMILES string

N[C@@H](Cc1ccc(F)cc1)C(O)=O

InChI key

XWHHYOYVRVGJJY-QMMMGPOBSA-N

InChI

1S/C9H10FNO2/c10-7-3-1-6(2-4-7)5-8(11)9(12)13/h1-4,8H,5,11H2,(H,12,13)/t8-/m0/s1

Gene Information

human ... TH(7054)
mouse ... TH(21823)
rat ... TH(25085)

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General description

Substrate for tyrosine hydroxylase that has been used to study the regulation of that enzyme. Substitution of p-fluorophenylalanine for phenylalanine in the culture medium inhibits mitosis and reversibly arrests HeLa cells in G2.

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signalword

Danger

hcodes

Hazard Classifications

Acute Tox. 2 Oral

存储类别

6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

法规信息

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分析证书(COA)

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P S Sunkara et al.
European journal of cell biology, 23(2), 312-316 (1981-02-01)
One of the objectives of this study was to develop a method for the reversible arrest of HeLa cells in G2 phase by using p-fluorophenylalanine (FPA), an analog of phenylalanine. Addition of 0.5 mM of FPA to synchronized HeLa cells
Elisa Benetti et al.
Metabolites, 10(5) (2020-05-24)
Recent findings indicate a significant association between sedentary (SED)-time and type 2 diabetes mellitus(T2DM). The aim of this study was to investigate whether different levels of SED-time could impact on biochemical and physiological processes occurring in sedentary and physically inactive
P J Hillas et al.
Biochemistry, 35(22), 6969-6975 (1996-06-04)
The iron-containing enzyme tyrosine hydroxylase catalyzes the hydroxylation of tyrosine to dihydroxyphenylalanine. A series of 4-X-substituted (X = H, F, Br, Cl, CH3, or CH3O) phenylalanines have been characterized as substrates to gain insight into the mechanism of hydroxylation. Multiple
R Shiman et al.
The Journal of biological chemistry, 269(40), 24637-24646 (1994-10-07)
Tetrahydropterins react with phenylalanine hydroxylase at a redox site, a regulatory site, and the catalytic site, but neither the properties of nor relationships among these sites are well understood. We have studied the redox site using the fluorescent iron chelators
Jing Yuan et al.
Nature chemical biology, 5(10), 765-771 (2009-09-08)
Studies of gene function and molecular mechanisms in Plasmodium falciparum are hampered by difficulties in characterizing and measuring phenotypic differences between individual parasites. We screened seven parasite lines for differences in responses to 1,279 bioactive chemicals. Hundreds of compounds were

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