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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 / Acetylglucosamine / Bacillus / Bacterial Proteins / Phosphoric Diester Hydrolases / Glucosamine / Membrane Proteins Language: En Journal: FEBS Lett Year: 1987 Type: Article
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Database: MEDLINE Main subject: Polyisoprenyl Phosphate Monosaccharides / Polyisoprenyl Phosphate Sugars / Acetylglucosamine / Bacillus / Bacterial Proteins / Phosphoric Diester Hydrolases / Glucosamine / Membrane Proteins Language: En Journal: FEBS Lett Year: 1987 Type: Article