Maurice J. Bessman

Maurice J. Bessman

Research Professor and Professor Emeritus

18 Biology East
410-516-7776
zoot@jhu.edu

Maurice Bessman received an A.B. from Harvard, an M.S. and PhD from Tufts, and a Post Doctoral fellowship at Washington University in St. Louis. He joined the department of Biology and the McCollum-Pratt Institute at Hopkins as an Assistant Professor in 1958, Professor in 1966, and Professor Emeritus and Research Professor in 2008.

We are currently studying the Nudix hydrolase family of enzymes. This is a large, widely distributed class of proteins that we have discovered having the common signature sequence:

GX6EX7REUXEEXU (U= Ile, Leu, or Val)

Over 600 members of the family have been identified in more than 200 species by BLAST searches of the data banks, and this number is increasing daily. We are systematically cloning selected members of the family, expressing them in E.coli, purifying the proteins and attempting to identify their function. This seemingly difficult task has been made practicable by our discovery that the common feature of the substrates of these enzymes is that they are all Nucleoside diphosphates linked to some other moiety, x, hence the acronym, Nudix. These enzymes can be thought of as surveillance proteins, because their substrates are either potentially toxic to the cell, are signaling molecules, or intermediates whose concentrations require modulation during cellular metabolism.

A UDP-X diphosphatase from Streptococcus pneumoniae hydrolyzes precursors of peptidoglycan biosynthesis. Duong-Ly KC, Woo HN, Dunn CA, Xu W, Babič A, Bessman MJ, Amzel LM, Gabelli SB., PLoS One. 2013

Structural studies of the Nudix GDP-mannose hydrolase from E. coli reveals a new motif for mannose recognition. Boto AN, Xu W, Jakoncic J, Pannuri A, Romeo T, Bessman MJ, Gabelli SB, Amzel LM., Proteins. 2011

The Nudix hydrolase CDP-chase, a CDP-choline pyrophosphatase, is an asymmetric dimer with two distinct enzymatic activities. Duong-Ly KC, Gabelli SB, Xu W, Dunn CA, Schoeffield AJ, Bessman MJ, Amzel LM., J Bacteriol. 2011

Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis. Gabelli SB, Bianchet MA, Xu W, Dunn CA, Niu ZD, Amzel LM, Bessman MJ., Structure. 2007

Three new Nudix hydrolases from Escherichia coli. Xu W, Dunn CA, O'handley SF, Smith DL, Bessman MJ., J Biol Chem. 2006

Legionella pneumophila NudA Is a Nudix hydrolase and virulence factor. Edelstein PH, Hu B, Shinzato T, Edelstein MA, Xu W, Bessman MJ. Infect Immun. 2005

The pnhA gene of Pasteurella multocida encodes a dinucleoside oligophosphate pyrophosphatase member of the Nudix hydrolase superfamily. Urick T, I-Chang C, Arena E, Xu W, Bessman MJ, Ruffolo CG. J Bacteriol. 2005

Gene ytkD of Bacillus subtilis encodes an atypical nucleoside triphosphatase member of the Nudix hydrolase superfamily. Xu W, Jones CR, Dunn CA, Bessman MJ., J Bacteriol. 2004

Structural studies of the Nudix hydrolase DR1025 from Deinococcus radiodurans and its ligand complexes. Ranatunga W, Hill EE, Mooster JL, Holbrook EL, Schulze-Gahmen U, Xu W, Bessman MJ, Brenner SE, Holbrook SR., J Mol Biol. 2004

The 26 Nudix hydrolases of Bacillus cereus, a close relative of Bacillus anthracis. Xu W, Dunn CA, Jones CR, D'Souza G, Bessman MJ. J Biol Chem. 2004