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
type
Grade II
Quality Level
form
salt-free, lyophilized powder
specific activity
300-1,500 units/mg protein
UniProt accession no.
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.
Analysis Note
Protein determined by biuret.
Other Notes
One unit will hydrolyze 1.0 μmole of N-acetyl-L-methionine per hr at pH 7.0 at 25 °C.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
低风险生物材料
动植物源性产品
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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)
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
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
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