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A3010

Sigma-Aldrich

Acylase I from porcine kidney

Grade I, lyophilized powder, ≥1500 units/mg protein

Sinónimos:

Aminoacylase, N-Acylamino acid amidohydrolase

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About This Item

Número de CAS:
9012-37-7
Comisión internacional de enzimas:
3.5.1.14 (BRENDA, IUBMB)
EC Number:
232-732-3
MDL number:
MFCD00081285
UNSPSC Code:
12352204
NACRES:
NA.54

type

Grade I

Quality Level

200

form

lyophilized powder

specific activity

≥1500 units/mg protein

composition

Protein, ≥60%

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 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)

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Y Fukagawa et al.
The Journal of antibiotics, 33(6), 543-549 (1980-06-01)
PS-5 was deacetylated to NS-5 (deacetylated PS-5) by l-amino acid acylase from porcine kidney and D-amino acid acylase from Streptomyces olivaceus but not by l-amino acid acylase from Aspergillus sp. Using PS-5, N-chloroacetyl-l-phenylalanine and N-chloroacetyl-D-valine as substrates, acylase producers were
Jinit Masania et al.
Oxidative medicine and cellular longevity, 2019, 4851323-4851323 (2019-12-13)
Glycation, oxidation, nitration, and crosslinking of proteins are implicated in the pathogenic mechanisms of type 2 diabetes, cardiovascular disease, and chronic kidney disease. Related modified amino acids formed by proteolysis are excreted in urine. We quantified urinary levels of these
K Kubo et al.
The Journal of antibiotics, 33(6), 556-565 (1980-06-01)
L-Amino acid acylase and D-amino acid acylase were stable below 50 degrees C, although the D-enzyme was more thermostable than the L-enzyme at higher temperatures. At 30 degrees C they showed the highest reaction velocity in phosphate buffer of pH
Debby Ngo et al.
JCI insight, 6(5) (2021-02-17)
Recent advances in proteomic technologies have made high-throughput profiling of low-abundance proteins in large epidemiological cohorts increasingly feasible. We investigated whether aptamer-based proteomic profiling could identify biomarkers associated with future development of type 2 diabetes (T2DM) beyond known risk factors.
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
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