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A8376

Sigma-Aldrich

Acylase I from porcine kidney

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

Synonym(s):

Aminoacylase, N-Acylamino acid amidohydrolase

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$249.00
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1 G
$249.00
10 G
$1,360.00

About This Item

CAS Number:
9012-37-7
Enzyme Commission number:
3.5.1.14 (BRENDA, IUBMB)
EC Number:
232-732-3
MDL number:
MFCD00081285
UNSPSC Code:
12352204
NACRES:
NA.54

$249.00

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type

Grade II

Quality Level

200

form

salt-free, lyophilized powder

specific activity

300-1,500 units/mg protein

UniProt accession no.

P37111

storage temp.

−20°C

Gene Information

pig ... ACY1(396930)

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Application

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 Actions

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]

Unit Definition

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

Analysis Note

Protein determined by biuret.

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
0000333389
0000333388
SLCK7012
SLBZ7228
SLBR0278V

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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)
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
Vildan Caner et al.
Antonie van Leeuwenhoek, 94(4), 527-532 (2008-07-31)
A total of 190 Campylobacter spp. isolates, of which 34 gave the result of very weak activity, and 156 gave the negative activity in the test for hippurate hydrolysis were characterized. The genomic DNA was isolated from a fresh culture
Tao Dong et al.
Bioresource technology, 101(16), 6569-6571 (2010-04-07)
The effects of bovine serum albumin (BSA) addition on the cross-linked enzyme aggregates (CLEA) of aminoacylase from Aspergillus melleus (EC 3.5.1.14) were conducted at varying glutaraldehyde to enzyme ratio. After optimization, CLEA of aminoacylase prepared with 10 mg BSA per
Shigekazu Yano et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 879(29), 3247-3252 (2011-05-07)
D-Aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 (AxD-NAase) offers a novel biotechnological application, the production of D-amino acid from the racemic mixture of N-acyl-DL-amino acids. However, its substrate specificity is biased toward certain N-acyl-D-amino acids. To construct mutant AxD-NAases with
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