CHARACTERIZATION AND SEQUENCE OF PHOC, THE PRINCIPAL PHOSPHATE-IRREPRESSIBLE ACID-PHOSPHATASE OF MORGANELLA-MORGANII
CHARACTERIZATION AND SEQUENCE OF PHOC, THE PRINCIPAL PHOSPHATE-IRREPRESSIBLE ACID-PHOSPHATASE OF MORGANELLA-MORGANII
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DOI：
10.1099/00221287-140-6-1341
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发表时间：
1994-06-01
期刊：
影响因子：
2.8
通讯作者：
ROSSOLINI, GM
中科院分区：
文献类型：
--
作者：
THALLER, MC;BERLUTTI, F;ROSSOLINI, GM
研究了为数不多的具有高水平磷酸不抑制酸性磷酸酶活性（HPAP表型）的莫organella morganii的磷酸酶活性，并克隆、测序了主要的磷酸不抑制酸性磷酸酶的编码基因，并对其产物进行了表征。利用对硝基苯磷酸作为底物，摩根菌产生了一种与HPAP表型相关的主要的磷酸不可抑制酸性磷酸酶（PhoC），一种次要的磷酸不可抑制酸性磷酸酶和一种磷酸可抑制碱性磷酸酶。当PhoC水解的有机磷酸酯（如2-磷酸甘油）是唯一的磷酸盐来源时，PhoC活性的存在阻止了碱性磷酸酶的诱导。PhoC是一种分泌的非特异性酸性磷酸酶，显然由4个25 kDa的多肽亚基组成。这种酶对EDTA、P-i、氟化物和酒石酸盐具有抗性。morganii的PhoC氨基酸序列与石华Providencia PhoN非特异性酸性磷酸酶的同源性为84.6%，与鼠伤寒沙门菌PhoN非特异性酸性磷酸酶的同源性为45.3%，与活动单胞菌的主酸性磷酸酶（PhoC）的同源性为37.8%。这些酶的序列数据和调控的比较表明，该基因家族成员在肠杆菌科中有不同的系统发育。
Phosphatase activities were investigated in Morganella morganii, which is one of the few enterobacterial species producing high-level phosphate-irrepressible acid phosphatase activity (HPAP phenotype), and the gene encoding the major phosphate-irrepressible acid phosphatase was cloned, sequenced, and its product characterized. Using p-nitrophenyl phosphate as substrate, Morganella produced a major phosphate-irrepressible acid phosphatase (named PhoC) which is associated with the HPAP phenotype, a minor phosphate-irrepressible acid phosphatase, and a phosphate-repressible alkaline phosphatase. The presence of the PhoC activity prevented induction of alkaline phosphatase when a PhoC-hydrolysable organic phosphate ester, such as glycerol 2-phosphate, was the sole phosphate source. PhoC is a secreted nonspecific acid phosphatase apparently composed of four 25 kDa polypeptide subunits. The enzyme is resistant to EDTA, P-i, fluoride and tartrate. The M. morganii PhoC showed 84.6% amino acid sequence identity to the PhoN nonspecific acid phosphatase of Providencia stuartii, 45.3% to the PhoN nonspecific acid phosphatase of Salmonella typhimurium, and 37.8% to the principal acid phosphatase (PhoC) of Zymomonas mobilis. Comparison of sequence data and of regulation of these enzymes suggested a different phylogeny of members of this gene family within the Enterobacteriaceae.