An enzyme catalyzing the liberation of N-acetylglucosamine from N-acetylglucosaminyl pyrophosphorylpolyprenol in Bacillus polymyxa membranes.
FEBS Lett
; 218(1): 131-4, 1987 Jun 22.
Article
in En
| MEDLINE
| ID: mdl-3036586
A novel enzyme which specifically hydrolyzes N-acetylglucosaminyl pyrophosphorylpolyprenol to liberate N-acetylglucosamine was found in membranes of Bacillus polymyxa AHU 1385. The enzyme seems to be inactive toward alpha-N-acetylglucosaminyl phosphorylundecaprenol, beta-N-acetylglucosaminyl phosphorylundecaprenol, N-acetylglucosamine 1-phosphate, N-acetylglucosamine 1-pyrophosphate, or UDP-N-acetylglucosamine. Much lower activities of the same enzyme were also found in membranes of several other strains of Bacilli.
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Database:
MEDLINE
Main subject:
Polyisoprenyl Phosphate Monosaccharides
/
Polyisoprenyl Phosphate Sugars
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Acetylglucosamine
/
Bacillus
/
Bacterial Proteins
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Phosphoric Diester Hydrolases
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Glucosamine
/
Membrane Proteins
Language:
En
Journal:
FEBS Lett
Year:
1987
Type:
Article