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Merck

A8376

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:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-732-3
MDL number:
EC Number:
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Product Name

Acylase I from porcine kidney, Grade II, salt-free, lyophilized powder, 300-1,500 units/mg protein

type

Grade II

form

salt-free, lyophilized powder

specific activity

300-1,500 units/mg protein

UniProt accession no.

storage temp.

−20°C

Quality Level

Gene Information

pig ... ACY1(396930)

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Analysis Note

Protein determined by biuret.

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.

Other Notes

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

pictograms

Health hazardExclamation mark

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

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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
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)
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
Yi Zhong et al.
Carcinogenesis, 30(1), 158-164 (2008-11-26)
A growing number of studies indicate a link between oxidative stress and cancer. We previously developed a rat model of renal cell carcinoma (RCC) induced by ferric nitrilotriacetate (Fe-NTA). Here, we performed a genome-wide analysis to study characteristics of genomic
Le Hoang Lam et al.
Talanta, 79(4), 1130-1134 (2009-07-21)
Assay of angiotensin I-converting enzyme (ACE) inhibitory activity always draws much attention because of diverse applications in the field of antihypertension and related pathogenesis. Recently, the use of a new synthetic substrate, 3-hydroxybutyrylglycyl-glycyl-glycine (3HB-GGG), for the assay of ACE inhibitory

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