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巨大芽孢杆菌S-腺苷-L-甲硫氨酸：尿卟啉原III甲基转移酶的一级结构、在大肠杆菌中的表达及性质

Primary structure, expression in Escherichia coli, and properties of S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase from Bacillus megaterium.

作者信息

Robin C, Blanche F, Cauchois L, Cameron B, Couder M, Crouzet J

机构信息

Institut des Biotechnologies, Rhône-Poulenc Rorer S.A., Vitry sur Seine, France.

出版信息

J Bacteriol. 1991 Aug;173(15):4893-6. doi: 10.1128/jb.173.15.4893-4896.1991.

DOI:10.1128/jb.173.15.4893-4896.1991
PMID:1906874
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC208169/
Abstract

A Bacillus megaterium DNA fragment encoding S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase (SUMT) activity was subcloned and sequenced. The encoded polypeptide showed more than 43.5% strict homology to Pseudomonas denitrificans SUMT (F. Blanche, L. Debussche, D. Thibaut, J. Crouzet, and B. Cameron, J. Bacteriol. 171:4222-4231, 1989). The B. megaterium polypeptide was overexpressed in Escherichia coli, partially purified, and shown to exhibit, like P. denitrificans SUMT, substrate inhibition at uroporphyrinogen III concentrations above 0.5 microM, suggesting a common regulation for aerobic cobalamin-producing organisms.

摘要

一个编码S-腺苷-L-甲硫氨酸：尿卟啉原III甲基转移酶（SUMT）活性的巨大芽孢杆菌DNA片段被亚克隆并测序。编码的多肽与反硝化假单胞菌SUMT显示出超过43.5%的严格同源性（F.布兰奇、L.德布舍、D.蒂博、J.克鲁泽和B.卡梅隆，《细菌学杂志》171:4222 - 4231，1989年）。巨大芽孢杆菌多肽在大肠杆菌中过表达，部分纯化，并显示出与反硝化假单胞菌SUMT一样，在尿卟啉原III浓度高于0.5微摩尔时表现出底物抑制，这表明需氧钴胺素产生菌存在共同的调控机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c94e/208169/a835e75845ed/jbacter00105-0355-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c94e/208169/9b51b45b4672/jbacter00105-0355-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c94e/208169/a835e75845ed/jbacter00105-0355-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c94e/208169/9b51b45b4672/jbacter00105-0355-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c94e/208169/a835e75845ed/jbacter00105-0355-b.jpg

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