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59891

Sigma-Aldrich

N-Acetyl-DL-β-phenylalanine

≥97.0% (HPLC)

Sinonimo/i:

Hydrocinnamic acid, (±)-3-(Acetylamino)-3-phenylpropionic acid

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About This Item

Formula empirica (notazione di Hill):
C11H13NO3
Numero CAS:
40638-98-0
Peso molecolare:
207.23
Beilstein:
2726794
Numero MDL:
MFCD00181164
Codice UNSPSC:
12352200
ID PubChem:
57651704

Saggio

≥97.0% (HPLC)

applicazioni

peptide synthesis

Stringa SMILE

CC(=O)NC(CC(O)=O)c1ccccc1

InChI

1S/C11H13NO3/c1-8(13)12-10(7-11(14)15)9-5-3-2-4-6-9/h2-6,10H,7H2,1H3,(H,12,13)(H,14,15)
HTWAFOFDKZAKQP-UHFFFAOYSA-N

Azioni biochim/fisiol

N-Acetyl-β-phenylalanine is a substrate for bacterial tRNA(Phe) peptidyltransferase. Hydrocinnamic acid is an aromatic lignin monomer.
N-Acetyl-DL-β-phenylalanine is a racemic mixture of N-acetylated β-phenylalanine enantiomers. N-Acetyl-DL-β-phenylalanine is a product generated from the chromogenic substrate N-acetyl-DL-phenylalanine β-napthyl ester by specific esterase(s).

Codice della classe di stoccaggio

13 - Non Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

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Certificati d'analisi (COA)

Lot/Batch Number
64558/1

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Jae-Jung Ko et al.
Bioresource technology, 100(4), 1622-1627 (2008-11-04)
This study is designed to investigate the biodegradation of high molecular weight (HMW) lignin under sulfate reducing conditions. With a continuously mesophilic operated reactor in the presence of co-substrates of cellulose, the changes in HMW lignin concentration and chemical structure
P K Tsung et al.
Biochimica et biophysica acta, 445(1), 112-117 (1976-08-12)
The chemotactic and N-acetyl-DL-phenylalanine beta-naphthyl esterase activities of rabbit peritoneal neutrophils are separable from each other by both DEAE cellulose and Sephadex G-100 column chromatography. Partially purified esterase obtained from DEAE-cellulose chromatography had molecular weight of 70 000. However, the
Anthony L Schilmiller et al.
The Plant journal : for cell and molecular biology, 60(5), 771-782 (2009-08-18)
The initial reactions of the phenylpropanoid pathway convert phenylalanine to p-coumaroyl CoA, a branch point metabolite from which many phenylpropanoids are made. Although the second enzyme of this pathway, cinnamic acid 4-hydroxylase (C4H), is well characterized, a mutant for the
T G Heckler et al.
Biochemistry, 27(19), 7254-7262 (1988-09-20)
Eight structurally modified peptidyl-tRNA(Phe),s were employed to study P-site binding and peptide bond formation in a cell-free system involving Escherichia coli ribosomes programmed with poly(uridylic acid). It was found that the two analogues (N-acetyl-D-phenylalanyl-tRNA(Phe) and N-acetyl-D-tyrosyl-tRNA(Phe] containing D-amino acids functioned
Heather D Coleman et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(11), 4501-4506 (2008-03-05)
p-Coumaroyl-CoA 3'-hydroxylase (C3'H) is a cytochrome P450-dependent monooxygenase that catalyzes the 3'-hydroxylation of p-coumaroyl shikimate and p-coumaroyl quinate. We used RNA interference to generate transgenic hybrid poplar suppressed in C3'H expression and analyzed them with respect to transcript abundance, cell
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