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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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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

type

Grade II

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 . Acylase I may be useful to catalyze N-acetyl amino acids to enantiomerically pure L-amino acids .

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. 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.

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)

Certificates of Analysis (COA)

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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
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
Keya Cai et al.
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 24(2), 285-290 (2008-05-10)
Three model silkworms, highly resistant strain, highly susceptible strain and their near isogenic line were established by hybridization and backcross. The resistance of silkworm (Bombyx mori L.) to BmNPV was studied at proteomic level using two-dimensional gel electrophoresis and MALDI
Xiaoyong Liu et al.
Journal of invertebrate pathology, 105(1), 84-90 (2010-05-18)
Silkworm hemolymph is an important defense tissue to resist bacteria and virus infections. To study the response of silkworm hemolymph in the resistance of Bombyx mori L. nucleopolyhedrovirus (BmNPV), we constructed a near-isogenic silkworm line with BmNPV resistance using highly
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