Publications by authors named "H Chebrou"
In this work, we have purified the His-tagged oxygenase (ht-oxygenase) component of Rhodococcus globerulus P6 biphenyl dioxygenase. The alpha or beta subunit of P6 oxygenase was exchanged with the corresponding subunit of Pseudomonas sp. strain LB400 or of Comamonas testosteroni B-356 to create new chimeras that were purified ht-proteins and designated ht-alpha(P6)beta(P6), ht-alpha(P6)beta(LB400), ht-alpha(P6)beta(B-356), ht-alpha(LB400)beta(P6), and ht-alpha(B-356)beta(P6).
View Article and Find Full Text PDFNorthern blotting analysis with RNA probes derived from amidase and nitrile hydratase genes from Rhodococcus sp. ACV2 revealed that both genes are part of the same operon. RNase protection mapping and sequence analysis indicated that the operon is probably under the control of a sigma 70-like promoter located upstream from the amidase gene.
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- The DNA sequence upstream of the amiE gene in Rhodococcus sp. R312 was analyzed, revealing a new open reading frame (ORF) called amiS2, which encodes a 206 amino acid protein with hydrophobic characteristics.
- The AmiS2 protein shares high similarity with proteins from Mycobacterium smegmatis, Pseudomonas aeruginosa, and Helicobacter pylori, and it likely contains seven transmembrane alpha-helices.
- The related amiB2 gene encodes a 351 amino acid protein with an ATP-binding motif and resembles the ATP-binding subunit of bacterial Clp protease, suggesting that both AmiB2 and AmiS2 are part of a novel family of ABC transporters
Article Synopsis
- Computer methods revealed strong similarities in amino-acid sequences among 21 amidases, all of which help break down organic nitrogen compounds and produce ammonia.
- A conserved motif was identified that could play a key role in how these enzymes bind to amides and function catalytically.
- The study also highlighted how genetic transfer mechanisms, like transposons and plasmids, may have helped spread these genes, providing insights into the evolution of these and related enzymes.
N-terminal amino acid sequence of mutant strain Brevibacterium sp. adipamidase.
Antonie Van Leeuwenhoek
January 1994
The adipamidase of a mutant strain Brevibacterium sp. R312 involved in the degradation of adiponitrile to adipic acid was purified. Its N-terminal amino acid sequence was shown to be identical to Brevibacterium sp.
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