P9208
Polymyxin Acylase from Pseudomonas sp.
≥0.1 units/mg solid
Synonym(s):
Peptide N-fatty acylase
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About This Item
Recommended Products
biological source
bacterial (Pseudomonas spp.)
Quality Level
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 and may be useful in cancer research since it has antitumor activity against murine and human tumor cells .
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 .
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.
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Customers Also Viewed
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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