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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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1 g
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CZK 7,910.00

About This Item

CAS Number:
9012-37-7
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-732-3
MDL number:
MFCD00081285
EC Number:
3.5.1.14 (BRENDA, IUBMB)
Specific activity:
300-1,500 units/mg protein

CZK 7,910.00

Please contact Customer Service for Availability
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type

Grade II

Quality Level

200

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)

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 [1]. Acylase I may be useful to catalyze N-acetyl amino acids to enantiomerically pure L-amino acids [2].

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.[1]

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.

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

Sigma-Aldrich

A8376

Acylase I from porcine kidney

Acylase I from porcine kidney Grade I, lyophilized powder, ≥1500 units/mg protein

Sigma-Aldrich

A3010

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Creatine Phosphokinase from rabbit muscle Type I, salt-free, lyophilized powder, ≥150 units/mg protein

Sigma-Aldrich

C3755

Creatine Phosphokinase from rabbit muscle

Creatininase from microorganisms lyophilized powder, 100-300 units/mg protein

Sigma-Aldrich

C3172

Creatininase from microorganisms

specific activity

300-1,500 units/mg protein

specific activity

≥1500 units/mg protein

specific activity

≥150 units/mg protein

specific activity

100-300 units/mg protein

Gene Information

pig ... ACY1(396930)

Gene Information

pig ... ACY1(396930)

Gene Information

-

Gene Information

-

form

salt-free, lyophilized powder

form

lyophilized powder

form

salt-free, lyophilized powder

form

lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

UniProt accession no.

P37111

UniProt accession no.

P37111

UniProt accession no.

-

UniProt accession no.

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

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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

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
0000531650
0000531650
0000333388
0000333389
0000333389

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Related Content

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
View All Related Papers

Global Trade Item Number

SKUGTIN
A8376-10G04061832754673
A8376-1G04061833391501

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