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A8376

Sigma-Aldrich

Acylase I aus Schweineniere

Grade II, salt-free, lyophilized powder, 300-1,500 units/mg protein

Synonym(e):

Aminoacylase, N-Acylaminosäure-Amidohydrolase

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1 G
243,00 €
10 G
1.570,00 €

243,00 €


Versandbereit am07. April 2025Details



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1 G
243,00 €
10 G
1.570,00 €

About This Item

CAS-Nummer:
EC-Nummer:
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

243,00 €


Versandbereit am07. April 2025Details


Typ

Grade II

Form

salt-free, lyophilized powder

Spezifische Aktivität

300-1,500 units/mg protein

UniProt-Hinterlegungsnummer

Lagertemp.

−20°C

Angaben zum Gen

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Anwendung

Acylase I from porcine kidney has been used to study the acylase I-catalyzed deacetylation of various S-alkyl-N-acetyl-L-cysteines and their carbon and oxygen analogues [1]. Acylase I may be useful to catalyze N-acetyl amino acids to enantiomerically pure L-amino acids [2].

Biochem./physiol. Wirkung

Acylase I is a zinc metalloprotein that catalyzes the kinetic resolution of unnatural and rarely occurring α-amino acids. Its enantioselectivity for the hydrolysis of N-acyl L-α-amino acids is nearly absolute, yet it accepts substrates having a wide range of structure and functionality.[3] Acylase I catalyzes the deacetylation of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines. n-Butylmalonic acid is an inhibitor of acylase I. S-alkyl-N-acetyl-L-cysteines with short (C0-C3) and unbranched S-alkyl substituents have been found to be good acylase I substrates.[1]

Einheitendefinition

One unit will hydrolyze 1.0 μmole of N-acetyl-L-methionine per hr at pH 7.0 at 25 °C.

Hinweis zur Analyse

Protein determined by biuret.

Piktogramme

Health hazardExclamation mark

Signalwort

Danger

Gefahreneinstufungen

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Zielorgane

Respiratory system

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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Kinetic resolution of unnatural and rarely occurring amino acids: enantioselective hydrolysis of N-acyl amino acids catalyzed by acylase I
Chenault HK, et al.
Journal of the American Chemical Society, 111(16), 6354-6364 (1989)
V Uttamsingh et al.
Chemical research in toxicology, 11(7), 800-809 (1998-07-22)
The aminoacylase that catalyzes the hydrolysis of N-acetyl-L-cysteine (NAC) was identified as acylase I after purification by column chromatography and electrophoretic analysis. Rat kidney cytosol was fractionated by ammonium sulfate precipitation, and the proteins were separated by ion-exchange column chromatography
A S Bommarius et al.
Annals of the New York Academy of Sciences, 672, 126-136 (1992-11-30)
The method of measuring enzyme deactivation by monitoring necessary addition of fresh enzyme to keep a constant degree of conversion in a CSTR at constant [E] x tau, the product of concentration of active enzyme [E] and residence time tau
Albert P Chen et al.
NMR in biomedicine, 24(5), 514-520 (2011-06-16)
Reporter-based cell detection and localization in vivo may become an important imaging tool with the emergence of cellular therapy. With the strong signal enhancement provided by dynamic nuclear polarization, an NMR-based reporter probe system utilizing specific enzyme expression and activity
Christoph M Ernst et al.
Molecular microbiology, 80(2), 290-299 (2011-02-11)
Bacteria are frequently exposed to cationic antimicrobial peptides (CAMPs) from eukaryotic hosts (host defence peptides) or from prokaryotic competitors (bacteriocins). However, many bacteria, among them most of the major human pathogens, achieve CAMP resistance by MprF, a unique enzyme that

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