![]() Ac-DL-β-Phe-OH structure
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Common Name | Ac-DL-β-Phe-OH | ||
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CAS Number | 40638-98-0 | Molecular Weight | 207.22600 | |
Density | 1.197g/cm3 | Boiling Point | 449.2ºC at 760 mmHg | |
Molecular Formula | C11H13NO3 | Melting Point | N/A | |
MSDS | USA | Flash Point | 225.5ºC |
Biodegradation of high molecular weight lignin under sulfate reducing conditions: lignin degradability and degradation by-products.
Bioresour. Technol. 100 , 1622-1627, (2009) 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 concentr... |
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RNAi-mediated suppression of p-coumaroyl-CoA 3'-hydroxylase in hybrid poplar impacts lignin deposition and soluble secondary metabolism.
Proc. Natl. Acad. Sci. U. S. A. 105 , 4501-4506, (2008) 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 expressio... |
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Mutations in the cinnamate 4-hydroxylase gene impact metabolism, growth and development in Arabidopsis.
Plant J. 60 , 771-782, (2009) 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 characte... |
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A simple method to determine trypsin and chymotrypsin inhibitory activity.
J. Biochem. Biophys. Methods 59 , 241-251, (2004) A colorimetric method for serine protease inhibition was modified using N-Acetyl-DL-Phenylalanine beta-Naphthylester (APNE) as the substrate and o-Dianisidine tetrazotized (oD) as the dye. The reaction generated a single peak absorbing at 530 nm for both tryp... |
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Ribosomal binding and dipeptide formation by misacylated tRNA(Phe),S.
Biochemistry 27 , 7254-7262, (1988) 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-p... |
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Chemotactic activity from rabbit peritoneal neutrophils. Lack of identity with N-acetyl-DL-phenylalanine beta-napthyl esterase.
Biochim. Biophys. Acta 445 , 112-117, (1976) 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-cell... |
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An association between Schistosoma mansoni worms and an enzymatically-active protease/peptidase in mouse blood.
Parasitology 135 , 467-472, (2008) An enzyme found previously in extracts of adult Schistosoma mansoni worms, that hydrolysed the chromogenic substrate N-acetyl-DL-phenylalanine beta-naphthyl-ester, has here been further investigated and characterized. Evidence that the molecule found in the p... |