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蜡样芽孢杆菌中的表观磷酸盐回收系统。

Apparent phosphate retrieval system in Bacillus cereus.

作者信息

Guddal P H, Johansen T, Schulstad K, Little C

机构信息

Department of Biochemistry, University of Tromsø, Norway.

出版信息

J Bacteriol. 1989 Oct;171(10):5702-6. doi: 10.1128/jb.171.10.5702-5706.1989.

Abstract

Bacillus cereus secretes three different phospholipases C. We studied the effect of Pi levels in the growth medium on the production of these exoenzymes. Production of both phosphatidylcholine-preferring phospholipase C and sphingomyelinase C was repressed by Pi in the growth medium, whereas production of phosphatidylinositol phospholipase C was unaffected. We also found that B. cereus secretes a phosphate-repressed alkaline phosphatase activity. Together with a previously reported highly efficient, active uptake system for Pi, these three phosphate-repressed exoenzyme activities seem to be part of a phosphate retrieval mechanism that operates under growth-limiting concentrations of Pi. In natural soil systems, which are the natural habitats of B. cereus, the scarcity of Pi is the major growth-limiting factor. A phosphate-repressed metalloprotease activity was also detected in culture supernatants of B. cereus. It is unclear whether this exoenzyme activity also participates in the proposed phosphate-scavenging system.

摘要

蜡样芽孢杆菌分泌三种不同的磷脂酶C。我们研究了生长培养基中磷水平对这些胞外酶产生的影响。生长培养基中的磷抑制了偏好磷脂酰胆碱的磷脂酶C和鞘磷脂酶C的产生,而磷脂酰肌醇磷脂酶C的产生不受影响。我们还发现蜡样芽孢杆菌分泌一种受磷抑制的碱性磷酸酶活性。连同先前报道的高效、活跃的磷摄取系统,这三种受磷抑制的胞外酶活性似乎是在磷生长限制浓度下运作的磷回收机制的一部分。在蜡样芽孢杆菌的自然栖息地——天然土壤系统中,磷的稀缺是主要的生长限制因素。在蜡样芽孢杆菌的培养上清液中也检测到一种受磷抑制的金属蛋白酶活性。尚不清楚这种胞外酶活性是否也参与了所提出的磷清除系统。

相似文献

1
Apparent phosphate retrieval system in Bacillus cereus.蜡样芽孢杆菌中的表观磷酸盐回收系统。
J Bacteriol. 1989 Oct;171(10):5702-6. doi: 10.1128/jb.171.10.5702-5706.1989.
9
Bacillus cereus phospholipase C: carboxylic acid ester specificity and stereoselectivity.
Biochim Biophys Acta. 1987 Jul 31;920(2):155-60. doi: 10.1016/0005-2760(87)90255-4.

本文引用的文献

8
Assay for phospholipase C.磷脂酶C测定
Methods Enzymol. 1981;72:347-51. doi: 10.1016/s0076-6879(81)72025-1.

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