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Key Documents

P9208

Sigma-Aldrich

Polymyxin Acylase from Pseudomonas sp.

≥0.1 units/mg solid

Synonym(s):

Peptide N-fatty acylase

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200 MG
₪7,082.00

₪7,082.00

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200 MG
₪7,082.00

About This Item

CAS Number:
111174-43-7
MDL number:
MFCD00286307
UNSPSC Code:
12352204
NACRES:
NA.54

₪7,082.00

Please contact Customer Service for Availability

biological source

bacterial (Pseudomonas spp.)

Quality Level

200

form

solid

specific activity

≥0.1 units/mg solid

relevant disease(s)

cancer

storage temp.

−20°C

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Application

Polymyxin acylase, from Pseudomonas sp., is a N-myristoyl cleaving enzyme that has been used to determine the N-myristoyl peptide sequence [1] and may be useful in cancer research since it has antitumor activity against murine and human tumor cells [2].

Biochem/physiol Actions

Polymyxin acylase, from Pseudomonas sp. deacylates polymyxin group antibiotics and long-chain fatty acyl groups of proteins. Polymyxin acylase has an affinity for long-chain fatty acyl proteins in human carcinoma cells [2].

Quality

Crude actone powder;

Unit Definition

One unit will hydrolyze 1 μmole of N-octanoyl-5-aminovaleric acid per min at pH 8.0 at 37°C.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
SLCF4395
SLCD7626
SLBZ8605
SLBT7841
SLBJ4412V

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Sigma-Aldrich

P4932

Polymyxin B sulfate salt

N Yasuda et al.
Biological & pharmaceutical bulletin, 18(4), 615-617 (1995-04-01)
Polymyxin acylase from Pseudomonas sp. M-6-3 can deacylate not only polymyxin group antibiotics, but also the long-chain fatty acyl group of proteins and peptides. We found the in vitro antitumor activity of polymyxin acylase against murine and human tumor cells
S Misumi et al.
Biochemical and biophysical research communications, 217(2), 632-639 (1995-12-14)
Polymyxin acylase isolated from Pseudomonas sp. M-6-3 was used as an N-myristoyl cleaving enzyme in order to determine a part of the N-terminal amino acid sequence of N-myristoyl proteins. The enzyme hydrolyzed a number of N-myristoyl oligopeptides at various hydrolysis

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