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地衣芽孢杆菌青霉素酶在大肠杆菌和枯草芽孢杆菌中的生物合成。

Biosynthesis of Bacillus licheniformis penicillinase in Escherichia coli and in Bacillus subtilis.

作者信息

Hayashi S, Wu H C

出版信息

J Bacteriol. 1983 Nov;156(2):773-7. doi: 10.1128/jb.156.2.773-777.1983.

DOI:10.1128/jb.156.2.773-777.1983
PMID:6415038
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC217895/
Abstract

Modified prepenicillinase was accumulated in both Escherichia coli and Bacillus subtilis treated with globomycin. Although the inhibitions of processings of prepenicillinase and prolipoprotein by globomycin in E. coli are qualitatively similar, they differ in the degree of inhibition at given concentrations of globomycin. The processing of prepenicillinase proceeds much more rapidly in E. coli than in B. subtilis.

摘要

用球霉素处理的大肠杆菌和枯草芽孢杆菌中均积累了修饰的青霉素酶原。虽然球霉素对大肠杆菌中青霉素酶原和前脂蛋白加工过程的抑制在性质上相似，但在给定浓度的球霉素下，它们在抑制程度上有所不同。青霉素酶原在大肠杆菌中的加工过程比在枯草芽孢杆菌中进行得快得多。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aac6/217895/071f7a485ca6/jbacter00240-0308-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aac6/217895/6b77952b436d/jbacter00240-0306-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aac6/217895/6e830e9a4cab/jbacter00240-0307-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aac6/217895/8afde35d714d/jbacter00240-0307-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aac6/217895/777cfe5e5a28/jbacter00240-0308-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aac6/217895/071f7a485ca6/jbacter00240-0308-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aac6/217895/6b77952b436d/jbacter00240-0306-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aac6/217895/6e830e9a4cab/jbacter00240-0307-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aac6/217895/8afde35d714d/jbacter00240-0307-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aac6/217895/777cfe5e5a28/jbacter00240-0308-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aac6/217895/071f7a485ca6/jbacter00240-0308-b.jpg

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Biosynthesis of Bacillus licheniformis penicillinase in Escherichia coli and in Bacillus subtilis.地衣芽孢杆菌青霉素酶在大肠杆菌和枯草芽孢杆菌中的生物合成。
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本文引用的文献

1
Post-translational modification and processing of Escherichia coli prolipoprotein in vitro.大肠杆菌前脂蛋白的体外翻译后修饰与加工
Proc Natl Acad Sci U S A. 1982 Apr;79(7):2255-9. doi: 10.1073/pnas.79.7.2255.
2
Lipoprotein nature of Bacillus licheniformis membrane penicillinase.地衣芽孢杆菌膜青霉素酶的脂蛋白性质
Proc Natl Acad Sci U S A. 1981 Jun;78(6):3511-5. doi: 10.1073/pnas.78.6.3511.
3
Bacillus licheniformis penicillinase synthesized in Escherichia coli contains covalently linked fatty acid and glyceride.在大肠杆菌中合成的地衣芽孢杆菌青霉素酶含有共价连接的脂肪酸和甘油酯。
J Bacteriol. 1985 Mar;161(3):949-54. doi: 10.1128/jb.161.3.949-954.1985.
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Modification, processing, and subcellular localization in Escherichia coli of the pCloDF13-encoded bacteriocin release protein fused to the mature portion of beta-lactamase.与β-内酰胺酶成熟部分融合的pCloDF13编码的细菌素释放蛋白在大肠杆菌中的修饰、加工及亚细胞定位
J Bacteriol. 1987 May;169(5):2245-50. doi: 10.1128/jb.169.5.2245-2250.1987.
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Processing of Bacillus licheniformis penicillinases lacking a lipoprotein modification site in Escherichia coli.
J Bacteriol. 1986 Mar;165(3):678-81. doi: 10.1128/jb.165.3.678-681.1986.
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Lipid modification of Escherichia coli penicillin-binding protein 3.大肠杆菌青霉素结合蛋白3的脂质修饰
J Bacteriol. 1988 Nov;170(11):5392-5. doi: 10.1128/jb.170.11.5392-5395.1988.
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Effect of a mutation preventing lipid modification on localization of the pCloDF13-encoded bacteriocin release protein and on release of cloacin DF13.一种阻止脂质修饰的突变对pCloDF13编码的细菌素释放蛋白定位及cloacin DF13释放的影响。
J Bacteriol. 1988 Sep;170(9):4153-60. doi: 10.1128/jb.170.9.4153-4160.1988.
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J Bioenerg Biomembr. 1990 Jun;22(3):451-71. doi: 10.1007/BF00763177.
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Signal peptidases and signal peptide hydrolases.信号肽酶和信号肽水解酶。
J Bioenerg Biomembr. 1990 Jun;22(3):271-90. doi: 10.1007/BF00763168.
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J Biol Chem. 1981 Mar 25;256(6):3125-9.
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