نتایج جستجو برای: carboxylases

تعداد نتایج: 235  

Journal: :The Journal of General Physiology 1942
M. G. Sevag M. Shelburne Stuart Mudd

The inhibiting effects of sulfonamide drugs and their derivatives on the anaerobic decarboxylation of pyruvic acid by Staphylococcus aureus, Escherichia coli, baker's and brewer's yeast, and a carboxylase preparation from brewer's yeast have been investigated. These drugs are: sulfanilamide, sulfapyridine, sulfadiazine, sulfamethyldiazine, sulfathiazole, sulfamethylthiazole, sulfanilamido-5-eth...

Journal: :Plant physiology 1972
C B Osmond

This paper reports effects of salts on in vitro activity of phosphoenolpyruvate carboxylase and ribulose-1,5-diphosphate carboxylase, isolated from species differing in salt tolerance.Inhibition of phosphoenolpyruvate carboxylase by the inorganic salts KCl, NaCl, and Na(4)SO(4) depended on the source of the enzyme. Phosphoenolpyruvate carboxylase isolated from leaves of C(4) plants was extremel...

Journal: :European Journal of Biochemistry 1993

Journal: :American journal of physiology. Cell physiology 2002
Dorothea M Peters Jacob B Griffin J Steven Stanley Mary M Beck Janos Zempleni

Biotin in breakdown products of biotinylated carboxylases serves as substrate for biotinylation of histones by biotinidase. Here we determined whether biotinylation of histones might play a role in repair of damaged DNA and in apoptosis. Jurkat cells were exposed to UV light to induce DNA damage. Abundance of thymine dimers increased about three times in response to UV exposure, consistent with...

2017
Matthew Bennett Martin Högbom

Biotin-dependent acetyl-CoA carboxylases catalyze the committed step in type II fatty acid biosynthesis, the main route for production of membrane phospholipids in bacteria, and are considered a key target for antibacterial drug discovery. Here we describe the first structure of AccA3, an essential component of the acetyl-CoA carboxylase system in Mycobacterium tuberculosis (MTb). The structure...

2008
Dorothy Beckett

Biotin influences transcription in organisms from bacteria to humans. The enzyme, biotin protein ligase, which catalyzes post-transcriptional biotin addition to biotin-dependent carboxylases, plays a central roll in transmitting the demand for biotin to gene expression. The molecular mechanism of this communication in bacteria is well understood and involves competing protein:protein interactio...

Journal: :Applied and Environmental Microbiology 2011

Journal: :Nature communications 2015
Ashley R Jurado Christine S Huang Xing Zhang Z Hong Zhou Liang Tong

Geranyl-CoA carboxylase (GCC) is essential for the growth of Pseudomonas organisms with geranic acid as the sole carbon source. GCC has the same domain organization and shares strong sequence conservation with the related biotin-dependent carboxylases 3-methylcrotonyl-CoA carboxylase (MCC) and propionyl-CoA carboxylase (PCC). Here we report the crystal structure of the 750-kDa α6β6 holoenzyme o...

Journal: :Plant physiology 1976
R H Brown T L Armitage M J Merrett

Ribulose 1,5-diphosphate carboxylase was isolated from Euglena gracilis Klebs strain Z Pringsheim, Chlorella fusca var. vacuolata, and Chlamydobotrys stellata, and the subunits from each enzyme were separated and purified by gel filtration on Sephadex G-200 in the presence of sodium dodecyl sulfate. Rabbit antibody was elicited against purified Euglena ribulose 1,5-diphosphate carboxylase whole...

Journal: :Cellular and Molecular Life Sciences 2012

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