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A8376

Acylase I aus Schweineniere

Grade II, salt-free, lyophilized powder, 300-1,500 units/mg protein

Synonym(e):

Aminoacylase, N-Acylaminosäure-Amidohydrolase

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Über diesen Artikel

CAS-Nummer:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-732-3
MDL number:
EG-Nummer:
Specific activity:
300-1,500 units/mg protein

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Unterstützung erhalten

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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Dieser Artikel
A3010C3755C3172
Gene Information

pig ... ACY1(396930)

Gene Information

pig ... ACY1(396930)

Gene Information

-

Gene Information

-

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

form

salt-free, lyophilized powder

form

lyophilized powder

form

salt-free, lyophilized powder

form

lyophilized powder

UniProt accession no.

P37111

UniProt accession no.

P37111

UniProt accession no.

-

UniProt accession no.

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

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.

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Lagerklasse

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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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
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
Albert P Chen et al.
NMR in biomedicine, 24(5), 514-520 (2011-06-16)
Reporter-based cell detection and localization in vivo may become an important imaging tool with the emergence of cellular therapy. With the strong signal enhancement provided by dynamic nuclear polarization, an NMR-based reporter probe system utilizing specific enzyme expression and activity
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

Verwandter Inhalt

Global Trade Item Number

SKUGTIN
A8376-10G04061832754673
A8376-1G04061833391501

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