Mycobacterium smegmatis

The enzyme from the bacterium Mycobacterium smegmatis is specific for maltose.

Mycobacterium goodii was previously known as Mycobacterium smegmatis group 2.

Giles is a bacteriophage that infects Mycobacterium smegmatis bacteria.

This enzyme is isolated from Mycobacterium smegmatis.

The trehalase enzyme of Mycobacterium smegmatis is a membrane bound protein .

A bacteriophage was found to infect Mycobacterium smegmatis in 1947 and was the first documented example of a mycobacteriophage.

This enzyme is involved in the formation of mannooligosaccharides in the membrane of Mycobacterium smegmatis.

Mycobacterium smegmatis is an acid-fast bacterial species in the phylum Actinobacteria and the genus Mycobacterium.

Mycobacterium smegmatis porin A (MspA) is the second biological nanopore currently being investigated for DNA sequencing.

Biosynthesis has been detected in Actinobacteria, such as Mycobacterium smegmatis and filamentous fungi, such as Neurospora crassa.

The topoisomerase I from Mycobacterium smegmatis has been demonstrated biochemically not to bind Zn(II) [ 34 ] .

NHEJ proteins have been identified in a number of bacteria, however, including Bacillus subtilis, Mycobacterium tuberculosis, and Mycobacterium smegmatis.

These results corroborate an earlier study that additionally reported antibacterial activity against Salmonella enterica serovar Typhimurium, Streptococcus pyogenes, and Mycobacterium smegmatis.

He and a Detroit colleague published two papers on studies with the bacterium Mycobacterium smegmatis, a fast-growing and non-pathogenic bacillus with similar physical properties to the tuberculosis bacillus.

Corndog and Omega, two related mycobacteriophages of Mycobacterium smegmatis, also encode Ku homologs and exploit the NHEJ pathway to recircularize their genomes during infection.

Joseph Katz and Aaron Lipsitz, Sodium Disecondary Butyl Naphthalene Sulphonate on the Growth of Mycobacterium smegmatis, J. Bacteriol.

While originally isolated from the bacterial species Mycobacterium smegmatis and Mycobacterium tuberculosis, the causative agent of tuberculosis, more than 2,400 mycobacteriophage have since been isolated from various environmental and clinical sources.

However, some bacteria such as Mycobacterium smegmatis as well as mammals and yeast use a type I synthase which is a large multifunctional protein similar to the synthase used for polyketide synthesis.

Recently, septum site determining protein (Ssd) was discovered in this bacteria as a septum inhibitor, leading to elongated cells (not only in this specie but also in and in Mycobacterium smegmatis).

A particularly rich natural source of F420 is Mycobacterium smegmatis, in which several dozen enzymes use F420 instead of the related cofactor FMN used by homologous enzymes in most other species.

The current research, conducted by Dr. Cole in collaboration with Dr. Ying Zhang of Hammersmith Hospital in London, used the organism mycobacterium smegmatis, which is closely related to the bacterium that causes human tuberculosis, but does not itself normally cause TB.

A 2005 study of the antimicrobial activity of several Lycoperdaceae revealed that Handkea utriformis has "significantly active" against a number of bacteria, including Bacillus subtilis, Escherichia coli, Klebsiella pneumonia, Pseudomonas aeruginosa, Salmonella typhimurium, Staphylococcus aureus, Streptococcus pyogenes, and Mycobacterium smegmatis.

Using a standard laboratory method to determine antimicrobial susceptibility, methanol-based extracts of Lycoperdon umbrinum fruit bodies were shown in a 2005 study to have "significant" antibacterial activity against various human pathogenic bacteria, including Bacillus subtilis, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, Streptococcus pyogenes, and Mycobacterium smegmatis.