The Nudix hydrolases of Deinococcus radiodurans.
All 21 of the Nudix hydrolase genes from the radiation-resistant organism Deinococcus radiodurans have been cloned into vectors under the control of T7 promoters and expressed as soluble proteins in Escherichia coli. Their sizes range from 9.8 kDa (91 amino acids) to 59 kDa (548 amino acids). Two novel proteins were identified, each with two Nudix boxes in its primary structure, unique among all other known Nudix hydrolases. Extracts of each of the expressed proteins were assayed by a generalized procedure that measures the hydrolysis of nucleoside diphosphate derivatives, and several enzymatic activities were tentatively identified. In addition to representatives of known Nudix hydrolase subfamilies active on ADP-ribose, NADH, dinucleoside polyphosphates or (deoxy)nucleoside triphosphates, two new enzymes, a UDP-glucose pyrophosphatase and a CoA pyrophosphatase, were identified.
Xu
W
W
Department of Biology and the McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, MD 21218, USA.
Shen
J
J
Dunn
C A
CA
Desai
S
S
Bessman
M J
MJ
D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology* / Q000528:radiation effects; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D011755:Pyrophosphatases / Q000235:genetics* / Q000378:metabolism*; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D000096964:Nudix Hydrolases
D011755:Pyrophosphatases; D000096964:Nudix Hydrolases