نتایج جستجو برای: sterptococcus thermophilus

تعداد نتایج: 2790  

2014
Laura Treu Veronica Vendramin Barbara Bovo Stefano Campanaro Viviana Corich Alessio Giacomini

This report describes the genome sequences of four Streptococcus thermophilus strains, namely, TH982, TH985, TH1477, and 1F8CT, isolated from different dairy environments from the Campania and the Veneto regions in Italy. These data are aimed at increasing the genomic information available on this species, which is of paramount importance for the dairy industry.

2016
Mohamed A. Zorgani Roland Quentin Marie-Frédérique Lartigue

Streptococcal species are Gram-positive bacteria involved in severe and invasive diseases in humans and animals. Although, this group includes different pathogenic species involved in life-threatening infections for humans, it also includes beneficial species, such as Streptococcus thermophilus, which is used in yogurt production. In bacteria virulence factors are controlled by various regulato...

Journal: :Applied and environmental microbiology 2003
Nuno Empadinhas Luciana Albuquerque Anke Henne Helena Santos Milton S da Costa

The biosynthetic pathway for the synthesis of the compatible solute alpha-mannosylglycerate (MG) in the thermophilic bacterium Thermus thermophilus HB27 was identified based on the activities of recombinant mannosyl-3-phosphoglycerate synthase (MPGS) (EC 2.4.1.217) and mannosyl-3-phosphoglycerate phosphatase (MPGP) (EC 3.1.3.70). The sequences of homologous genes from the archaeon Pyrococcus ho...

Journal: :Applied and environmental microbiology 1998
T Kosuge T Hoshino

Growth of Thermus thermophilus HB27 was inhibited by a proline analog, 3,4-dehydroproline (DHP). This result suggested that the gamma-glutamyl kinase (the product of the proB gene) was inhibited by feedback inhibition in T. thermophilus. DHP-resistant mutants were reported previously for Escherichia coli (A. M. Dandekar and S. L. Uratsu, J. Bacteriol. 170:5943-5945, 1988) and Serratia marcescen...

Journal: :Bioscience, biotechnology, and biochemistry 2010
Ryoko Sano Masafumi Kameya Satoshi Wakai Hiroyuki Arai Yasuo Igarashi Masaharu Ishii Yoshihiro Sambongi

The thermo-neutrophilic hydrogen-oxidizing bacterium Hydrogenobacter thermophilus constitutively oxidizes thiosulfate. Soluble extracts of it showed temperature-dependent thiosulfate oxidation activity with an optimum at 60 degrees C. A gene cluster for sox (sulfur oxidation) is presumably responsible for this activity. Among the cluster, two tandemly coded soxA genes were uniquely found. These...

Journal: :Journal of biochemistry 2001
H Ura K Harata I Matsui S Kuramitsu

We determined the crystal structure of the liganded form of alpha-aminotransferase from a hyperthermophile, Pyrococcus horikoshii. This hyperthermophilic enzyme did not show domain movement upon binding of an acidic substrate, glutamate, except for a small movement of the alpha-helix from Glu16 to Ala25. The omega-carboxyl group of the acidic substrate was recognized by Tyr70* without its side-...

Journal: :The Journal of biological chemistry 2007
Tommi A White Navasona Krishnan Donald F Becker John J Tanner

Proline dehydrogenase (PRODH) and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH) catalyze the two-step oxidation of proline to glutamate. They are distinct monofunctional enzymes in all eukaryotes and some bacteria but are fused into bifunctional enzymes known as proline utilization A (PutA) in other bacteria. Here we report the first structure and biochemical data for a monofunctional ...

Journal: :The Journal of biological chemistry 1998
Y Nobe S Kawaguchi H Ura T Nakai K Hirotsu R Kato S Kuramitsu

Aspartate aminotransferase (AspAT) is a unique enzyme that can react with two types of substrate with quite different properties, acidic substrates, such as aspartate and glutamate, and neutral substrates, although the catalytic group Lys-258 acts on both types of substrate. The dynamic properties of the substrate-binding site are indispensable to the interaction with hydrophobic substrates (Ka...

Journal: :Microbial Cell Factories 2006
Gabriele Giliberti Loredana Baccigalupi Angelina Cordone Ezio Ricca Maurilio De Felice

BACKGROUND RecA is a highly conserved prokaryotic protein that not only plays several important roles connected to DNA metabolism but also affects the cell response to various stress conditions. While RecA is highly conserved, the mechanism of transcriptional regulation of its structural gene is less conserved. In Escherichia coli the LexA protein acts as a recA repressor and is able, in respon...

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