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
Sign Into View Organizational & Contract Pricing
All Photos(2)
About This Item
Recommended Products
type
Grade II
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)
Looking for similar products? Visit Product Comparison Guide
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.
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
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
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
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
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
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service