Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery
Publication Date : //
Antibiotic resistance is a major issue in the treatment of infectious diseases such as tuberculosis. Existing antibiotics target only a few cellular pathways and there is an urgent need for antibiotics that have novel molecular mechanisms. The glmU gene is essential in Mycobacterium tuberculosis, being required for optimal bacterial growth, and has been selected as a possible drug target for structural and functional investigation. GlmU is a bifunctional acetyltransferase/uridyltransferase that catalyses the formation of UDP-GlcNAc from GlcN-1-P. UDP-GlcNAc is a substrate for two important biosynthetic pathways: lipopolysaccharide and peptidoglycan synthesis. The crystal structure of M. tuberculosis GlmU has been determined in an unliganded form and in complex with GlcNAc-1-P or UDP-GlcNAc. The structures reveal the residues that are responsible for substrate binding. Enzyme activities were characterized by (1)H NMR and suggest that the presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity.
Authors : Zhang Zhening , Bulloch Esther M M , Bunker Richard D , Baker Edward N , Squire Christopher J ,
Related products :
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88
Logistic :0241 40 08 90 86
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
email@example.com | Gentaur | Gentaur
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123
Canada Montreal +15149077481
Ceská republika Praha +420246019719
Finland Helsset +358942419041
Magyarország Budapest +3619980547
US New York+17185132983
WP1619: Amino sugar and nucleotide sugar metabolism
Related Genes :
 Computationally Guided Identification of Novel Mycobacterium tuberculosis GlmU Inhibitory Leads, Their Optimization, and in Vitro Validation.
 High-throughput screen identifies small molecule inhibitors targeting acetyltransferase activity of Mycobacterium tuberculosis GlmU.
 Structure-based design of diverse inhibitors of Mycobacterium tuberculosis N-acetylglucosamine-1-phosphate uridyltransferase: combined molecular docking, dynamic simulation, and biological activity.
 Structural and functional features of enzymes of Mycobacterium tuberculosis peptidoglycan biosynthesis as targets for drug development.
 Inhibition studies on Mycobacterium tuberculosis N-acetylglucosamine-1-phosphate uridyltransferase (GlmU).
 Substrate-bound crystal structures reveal features unique to Mycobacterium tuberculosis N-acetyl-glucosamine 1-phosphate uridyltransferase and a catalytic mechanism for acetyl transfer.
 Identification of amino acids involved in catalytic process of M. tuberculosis GlmU acetyltransferase.
 Design and synthesis of novel cell wall inhibitors of Mycobacterium tuberculosis GlmM and GlmU.
 Structure and mutational analysis of the archaeal GTP:AdoCbi-P guanylyltransferase (CobY) from Methanocaldococcus jannaschii: insights into GTP binding and dimerization.
 Unraveling the potential of intrinsically disordered proteins as drug targets: application to Mycobacterium tuberculosis.
Enter catalog number :