135046
4-Nitrophenyl trimethylacetate
98%
Sinonimo/i:
4-Nitrophenyl pivalate
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About This Item
Formula condensata:
(CH3)3CCO2C6H4NO2
Numero CAS:
Peso molecolare:
223.23
Numero MDL:
Codice UNSPSC:
12352100
ID PubChem:
NACRES:
NA.22
Prodotti consigliati
Saggio
98%
Forma fisica
solid
Punto di fusione
92-95 °C (lit.)
Stringa SMILE
CC(C)(C)C(=O)Oc1ccc(cc1)[N+]([O-])=O
InChI
1S/C11H13NO4/c1-11(2,3)10(13)16-9-6-4-8(5-7-9)12(14)15/h4-7H,1-3H3
QADVJDGFQGNSIF-UHFFFAOYSA-N
Descrizione generale
4-Nitrophenyl trimethylacetate undergoes hydrolysis catalysed by cytoplasmic aldehyde dehydrogenase in presence of NAD+, NADH, propionaldehyde, chloral hydrate, diethylstilboestrol and p-nitrobenzaldehyde (modifiers).
Applicazioni
4-Nitrophenyl trimethylacetate was used as sensitive probe to study the catalytic activity of carboxypeptidase Y.
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
The trimethylacetyl-transglutaminase complex.
J E Folk
Methods in enzymology, 87, 36-42 (1982-01-01)
Studies of the esterase activity of cytosolic aldehyde dehydrogenase using sterically hindered and cyclic substrates.
K E Kitson et al.
Advances in experimental medicine and biology, 372, 45-52 (1995-01-01)
T M Kitson
The Biochemical journal, 257(2), 573-578 (1989-01-15)
The effects of modifiers (NAD+, NADH, propionaldehyde, chloral hydrate, diethylstilboestrol and p-nitrobenzaldehyde) on the hydrolysis of p-nitrophenyl (PNP) pivalate (PNP trimethylacetate) catalysed by cytoplasmic aldehyde dehydrogenase are reported. In each case a different inhibition pattern is obtained to that observed
H C Margolis et al.
The Journal of biological chemistry, 253(21), 7891-7897 (1978-11-10)
In the course of our further investigation of the active site titration of carboxypeptidase Y, using 4-nitrophenyl trimethylacetate, we have found that carboxypeptidase Y can be isolated in different molecular forms. Carboxypeptidase Y obtained from Fleischmann baker's yeast has a
Roall Espersen et al.
Applied microbiology and biotechnology, 104(6), 2513-2522 (2020-01-29)
Two proteases, named C- and T-like proteases, respectively, were purified from the culture supernatant of Amycolatopsis keratinophila subsp. keratinophila D2T grown on a keratinous slaughterhouse by-product of pig bristles and nails as sole nitrogen and carbon source. The two proteases
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