Zobrazeno 1 - 10
of 94
pro vyhledávání: '"Maurice J Bessman"'
Autor:
Krisna C Duong-Ly, Hyun Nyun Woo, Christopher A Dunn, WenLian Xu, Andrej Babič, Maurice J Bessman, L Mario Amzel, Sandra B Gabelli
Publikováno v:
PLoS ONE, Vol 8, Iss 5, p e64241 (2013)
The gene for a Nudix enzyme (SP_1669) was found to code for a UDP-X diphosphatase. The SP_1669 gene is localized among genes encoding proteins that participate in cell division in Streptococcus pneumoniae. One of these genes, MurF, encodes an enzyme
Externí odkaz:
https://doaj.org/article/b687255e82034ddba3d3e7e239bce26c
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 77:a281-a281
Autor:
Archana Pannuri, Tony Romeo, Maurice J. Bessman, Sandra B. Gabelli, WenLian Xu, Agedi N. Boto, L. Mario Amzel, Jean Jakoncic
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:2455-2466
The Nudix hydrolase superfamily, characterized by the presence of the signature sequence GX(5)EX(7)REUXEEXGU (where U is I, L, or V), is a well-studied family in which relations have been established between primary sequence and substrate specificity
Publikováno v:
Journal of Bacteriology. 186:8380-8384
Gene ytkD of Bacillus subtilis , a member of the Nudix hydrolase superfamily, has been cloned and expressed in Escherichia coli . The purified protein has been characterized as a nucleoside triphosphatase active on all of the canonical ribo- and deox
Publikováno v:
Journal of Biological Chemistry. 279:24861-24865
The genome of Bacillus cereus contains 26 Nudix hydrolase genes, second only to its closest relative, Bacillus anthracis which has 30. All 26 genes have been cloned, 25 have been expressed, and 21 produced soluble proteins suitable for analysis. Subs
Autor:
Elizabeth L. Holbrook, Ursula Schulze-Gahmen, Maurice J. Bessman, WenLian Xu, Stephen R. Holbrook, Wasantha Ranatunga, Emma Hill, Jana L. Mooster, Steven E. Brenner
Publikováno v:
Journal of Molecular Biology. 339:103-116
We have determined the crystal structure, at 1.4 A, of the Nudix hydrolase DR1025 from the extremely radiation resistant bacterium Deinococcus radiodurans. The protein forms an intertwined homodimer by exchanging N-terminal segments between chains. W
Publikováno v:
Journal of Biological Chemistry. 278:37492-37496
A new subfamily of the Nudix hydrolases, identified by conserved amino acids upstream and downstream of the Nudix box, has been characterized. The cloned, expressed, and purified orthologous enzymes have major activities on the non-canonical nucleosi
Autor:
Anne-Laure Perraud, Andrew M. Scharenberg, Karsten Rippe, Betty W. Shen, Maurice J. Bessman, Megan K. Smith, Christopher A. Dunn, Barry L. Stoddard
Publikováno v:
Journal of Biological Chemistry. 278:1794-1801
We have recently characterized the protein product of the human NUDT9 gene as a highly specific ADP-ribose (ADPR) pyrophosphatase. We now report an analysis of the human NUDT9 gene and its potential alternative transcripts along with detailed studies
Publikováno v:
Biochemistry. 41:9279-9285
Escherichia coli ADP-ribose (ADPR) pyrophosphatase (ADPRase), a Nudix enzyme, catalyzes the Mg(2+)-dependent hydrolysis of ADP-ribose to AMP and ribose 5-phosphate. ADPR hydrolysis experiments conducted in the presence of H(2)(18)O and analyzed by el
Publikováno v:
Molecular & Cellular Proteomics. 1:179-185
The genomic sequence of Rickettsia prowazekii, the obligate intracellular bacterium responsible for epidemic typhus, reveals an uncharacterized invasion gene homolog (invA). The deduced protein of 18,752 Da contains a Nudix signature, the specific mo