The Nudix hydrolases of Deinococcus radiodurans.

Abstract:

: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.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Xu W,Shen J,Dunn CA,Desai S,Bessman MJ

doi

10.1046/j.1365-2958.2001.02267.x

subject

Has Abstract

pub_date

2001-01-01 00:00:00

pages

286-90

issue

2

eissn

0950-382X

issn

1365-2958

pii

mmi2267

journal_volume

39

pub_type

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