Zobrazeno 1 - 10
of 101
pro vyhledávání: '"Norma M, Allewell"'
Publikováno v:
PLoS ONE, Vol 8, Iss 7, p e70369 (2013)
N-acetylglutamate synthase (NAGS) catalyzes the conversion of AcCoA and L-glutamate to CoA and N-acetyl-L-glutamate (NAG), an obligate cofactor for carbamyl phosphate synthetase I (CPSI) in the urea cycle. NAGS deficiency results in elevated levels o
Externí odkaz:
https://doaj.org/article/c04939634cc44988a43f269b9a8255cd
Autor:
Dashuang Shi, Yongdong Li, Juan Cabrera-Luque, Zhongmin Jin, Xiaolin Yu, Gengxiang Zhao, Nantaporn Haskins, Norma M Allewell, Mendel Tuchman
Publikováno v:
PLoS ONE, Vol 6, Iss 12, p e28825 (2011)
Novel bifunctional N-acetylglutamate synthase/kinases (NAGS/K) that catalyze the first two steps of arginine biosynthesis and are homologous to vertebrate N-acetylglutamate synthase (NAGS), an essential cofactor-producing enzyme in the urea cycle, we
Externí odkaz:
https://doaj.org/article/de8dae987bdc4042b99fb83b43ae9ad3
Publikováno v:
International Journal of Molecular Sciences, Vol 16, Iss 8, Pp 18836-18864 (2015)
International Journal of Molecular Sciences
International Journal of Molecular Sciences
Enzymes in the transcarbamylase family catalyze the transfer of a carbamyl group from carbamyl phosphate (CP) to an amino group of a second substrate. The two best-characterized members, aspartate transcarbamylase (ATCase) and ornithine transcarbamyl
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 16, Iss 6, Pp 13004-13022 (2015)
Volume 16
Issue 6
Pages 13004-13022
International Journal of Molecular Sciences, Vol 16, Iss 6, Pp 13004-13022 (2015)
Volume 16
Issue 6
Pages 13004-13022
N-acetylglutamate synthase (NAGS) catalyzes the production of N-acetylglutamate (NAG) from acetyl-CoA and l-glutamate. In microorganisms and plants, the enzyme functions in the arginine biosynthetic pathway, while in mammals, its major role is to pro
Autor:
Gengxiang Zhao, Dashuang Shi, Mendel Tuchman, Zhongmin Jin, Norma M. Allewell, Nantaporn Haskins
Publikováno v:
Biochemical and Biophysical Research Communications. 437:585-590
Maricaulis maris N-acetylglutamate synthase/kinase (mmNAGS/K) catalyzes the first two steps in l -arginine biosynthesis and has a high degree of sequence and structural homology to human N-acetylglutamate synthase, a regulator of the urea cycle. The
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 81:1847-1854
We report herein the crystal structure of Escherichia coli RimK at a resolution of 2.85 A, an enzyme that catalyzes the post-translational addition of up to 15 C-terminal glutamate residues to ribosomal protein S6. The structure belongs to the ATP-gr
Publikováno v:
Biochemical and Biophysical Research Communications. 430:1253-1258
N -acetyl-L-glutamate synthase catalyzes the conversion of AcCoA and glutamate to CoA and N-acetyl-L-glutamate (NAG), the first step of the arginine biosynthetic pathway in lower organisms. In mammals, NAG is an obligate cofactor of carbamoyl phospha
Autor:
Norma M. Allewell
Publikováno v:
The Journal of biological chemistry. 291(24)
The biofilms that many bacteria and fungi produce enable them to form communities, adhere tightly to surfaces, evade host immunity, and resist antibiotics. Pathogenic microorganisms that form biofilms are very difficult to eradicate and thus are a fr
Autor:
Xiaolin Yu, Mendel Tuchman, Gengxiang Zhao, Dashuang Shi, Jeremy Ho, Norma M. Allewell, Shennon Lu
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 80:1436-1447
Putrescine carbamoyltransferase (PTCase) catalyzes the conversion of carbamoylputrescine to putrescine and carbamoyl phosphate (CP), a substrate of carbamate kinase (CK). The crystal structure of PTCase has been determined and refined at 3.2 A resolu
Autor:
Xiaolin Yu, Hiroki Morizono, Mendel Tuchman, Vatsala Sagar, Dashuang Shi, Norma M. Allewell, Ljubica Caldovic, Zhongmin Jin
Publikováno v:
Journal of Biological Chemistry. 283:7176-7184
The crystal structures of N-acetylglutamate synthase (NAGS) in the arginine biosynthetic pathway of Neisseria gonorrhoeae complexed with acetyl-CoA and with CoA plus N-acetylgluta-mate have been determined at 2.5- and 2.6-Å resolution, respectively.