Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Farah Javid-Majd"'
Publikováno v:
Journal of Molecular Biology. 355:784-797
Mycobacterium tuberculosis , the cause of tuberculosis, presents a major threat to human health worldwide. Biosynthetic enzymes that are essential for the survival of the bacterium, especially in activated macrophages, are important potential drug ta
Autor:
S. Ye, Gregory D. Reinhart, N.M. Paricharttanakul, Farah Javid-Majd, Ann L. Menefee, James C. Sacchettini
Publikováno v:
Biochemistry. 44:15280-15286
Phosphofructokinase from Lactobacillus delbrueckii subspecies bulgaricus (LbPFK) has been reported to be a nonallosteric analogue of phosphofructokinase from Escherichia coli at pH 8.2 [Le Bras et al. (1991) Eur. J. Biochem. 198, 683-687]. A reexamin
Publikováno v:
Journal of Biological Chemistry. 275:5073-5080
Carbamoyl-phosphate synthetase (CPS) from Escherichia coli is a heterodimeric protein. The larger of the two subunits (M(r) approximately 118,000) contains a pair of homologous domains of approximately 400 residues each that are approximately 40% ide
Autor:
Marilyn F. Harmon, Farah Javid-Majd, Michelle A. Stapleton, Frank M. Raushel, Jennifer L. Grahmann, Brent A. Hanks, Leisha S. Mullins
Publikováno v:
Biochemistry. 35:14352-14361
Carbamoyl phosphate synthetase (CPS) catalyzes the formation of carbamoyl phosphate from glutamine, bicarbonate, and 2 mol of MgATP. The heterodimeric protein is composed of a small amidotransferase subunit and a larger synthetase subunit. The synthe
Phosphoribosyl-ATP pyrophosphohydrolase is the second enzyme in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP to phosphoribosyl-AMP and pyrophosphate. It is encoded by the hisE gene, which is present as a separate ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e116d9ac5bc3a0a11eb18b8a6d8bc8ff
https://europepmc.org/articles/PMC2631106/
https://europepmc.org/articles/PMC2631106/
Publikováno v:
Nature structural biology. 9(9)
AAC(2')-Ic catalyzes the coenzyme A (CoA)-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides. The crystal structure of the AAC(2')-Ic from Mycobacterium tuberculosis has been determined in the apo enzyme fo
Publikováno v:
Archives of biochemistry and biophysics. 400(1)
Ornithine is an allosteric activator of carbamoyl phosphate synthetase (CPS) from Escherichia coli. Nine amino acids in the vicinity of the binding sites for ornithine and potassium were mutated to alanine, glutamine, or lysine. The residues E783, T1
Publikováno v:
The Journal of biological chemistry. 276(49)
The chromosomally encoded aminoglycosideN-acetyltransferase, AAC(2′)-Ic, of Mycobacterium tuberculosis has a yet unidentified physiological function. Theaac(2′)-Ic gene was cloned and expressed inEscherichia coli, and AAC(2′)-Ic was purified. R
Autor:
John S. Blanchard, Farah Javid-Majd
Publikováno v:
Biochemistry. 39(6)
The E. coli argE-encoded N-acetyl-L-ornithine deacetylase has been cloned, expressed, and purified in high yield. The substrate specificity of the enzyme is relatively broad, with a number of alpha-N-acyl-L-amino acids exhibiting activity, including
Autor:
Michelle A. Stapleton, Brent A. Hanks, Frank M. Raushel, Leisha S. Mullins, Farah Javid-Majd, Marilyn F. Harmon
Publikováno v:
Biochemistry. 35(45)
Carbamoyl phosphate synthetase (CPS) from Escherichia coli catalyzes the formation of carbamoyl phosphate from two molecules of MgATP, bicarbonate, and glutamine. It has been previously shown that the amino- and carboxy-terminal halves of the large s