Araki Y, Oba S, Araki S, Ito E
J Biochem. 1980 Aug;88(2):469-79. doi: 10.1093/oxfordjournals.jbchem.a132994.
An enzyme which catalyzes the hydrolysis of acetamido groups of N-acetylglucosamine residues in cell wall peptidoglycan was found in the supernatant and 20,000 X g pellet fractions of Bacillus cereus. Autolysis of the latter fraction resulted in solubilization and activation of the deacetylase. Among various bacteria, strains of B. cereus which contain high proportions of N-unsubstituted glucosamine residues in their cell wall peptidoglycan components are particularly rich in the deacetylase. The peptidoglycan deacetylase is distinguishable from N-acetylglucosamine-6-phosphate deacetylase [EC 3.5.1.25] on the basis of their cellular distribution and chromatographic behavior. The rate of reaction of the deacetylase with (N-acetylglucosaminyl-N-acetylmuramic acid)3 [abbreviated as (GlcNAc-MurNAc)3] is less than 1/100 of that with peptidoglycan, while the enzyme is inactive towards (GlcNAc-MurNAc)2, GlcNAc-MurNAc, and monomeric N-acetylglucosamine derivatives. The enzyme also deacetylates partially O-hydroxyethylated chitin. The concentrations of peptidoglycan and partially O-hydroxyethylated chitin required for half-maximum activities were found to be 0.29 and 6.9 mg per ml (or 0.17 and 20 mM with respect to N-acetylglucosamine residues), respectively. The occurrence of this enzyme accounts for the formation of cell wall peptidoglycan N-unsubstituted at the glucosamine residues.
在蜡样芽孢杆菌的上清液和20,000×g沉淀组分中发现了一种酶，该酶可催化细胞壁肽聚糖中N - 乙酰葡糖胺残基的乙酰胺基水解。后一组分的自溶导致脱乙酰酶的溶解和激活。在各种细菌中，细胞壁肽聚糖成分中含有高比例N - 未取代葡糖胺残基的蜡样芽孢杆菌菌株，其脱乙酰酶含量特别丰富。基于其细胞分布和色谱行为，肽聚糖脱乙酰酶与N - 乙酰葡糖胺 - 6 - 磷酸脱乙酰酶[EC 3.5.1.25]不同。脱乙酰酶与（N - 乙酰葡糖胺基 - N - 乙酰胞壁酸）3[简称为（GlcNAc - MurNAc）3]的反应速率不到与肽聚糖反应速率的1/100，而该酶对（GlcNAc - MurNAc）2、GlcNAc - MurNAc和单体N - 乙酰葡糖胺衍生物无活性。该酶还可使部分O - 羟乙基化的几丁质脱乙酰。发现半最大活性所需的肽聚糖和部分O - 羟乙基化几丁质的浓度分别为每毫升0.29和6.9毫克（或相对于N - 乙酰葡糖胺残基为0.17和20 mM）。这种酶的存在解释了细胞壁肽聚糖在葡糖胺残基处N - 未取代的形成。
