2005
DOI: 10.1128/jb.187.14.4984-4991.2005
|View full text |Cite
|
Sign up to set email alerts
|

Systematic Characterization of the ADP-Ribose Pyrophosphatase Family in the Cyanobacterium Synechocystis sp. Strain PCC 6803

Abstract: We have characterized four putative ADP-ribose pyrophosphatases Sll1054, Slr0920, Slr1134, and Slr1690 in the cyanobacterium Synechocystis sp. strain PCC 6803. Each of the recombinant proteins was overexpressed in Escherichia coli and purified. Sll1054 and Slr0920 hydrolyzed ADP-ribose specifically, while Slr1134 hydrolyzed not only ADP-ribose but also NADH and flavin adenine dinucleotide. By contrast, Slr1690 showed very low activity for ADP-ribose and had four substitutions of amino acids in the Nudix motif,… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

1
9
0

Year Published

2008
2008
2019
2019

Publication Types

Select...
8
1

Relationship

0
9

Authors

Journals

citations
Cited by 9 publications
(10 citation statements)
references
References 38 publications
1
9
0
Order By: Relevance
“…8). This is consistent with an earlier description of the Nudix hydrolase Slr1690 from Cyanobacterium species (32). Thus, it is plausible that the presence of an intact Nudix signature sequence is essential for the catalytic activity of a typical member of bifunctional NrtR.…”
Section: Resultssupporting
confidence: 93%
“…8). This is consistent with an earlier description of the Nudix hydrolase Slr1690 from Cyanobacterium species (32). Thus, it is plausible that the presence of an intact Nudix signature sequence is essential for the catalytic activity of a typical member of bifunctional NrtR.…”
Section: Resultssupporting
confidence: 93%
“…Besides possessing a completely different fold, COG1058 ADPRPs show unique Co +2 - and K + -dependence, with an optimum pH at 7.5, whereas Nudix ADPRPs are either Mg +2 - or Mn +2 -dependent, with a more alkaline optimum pH [34]. Nevertheless, COG1058 ADPRPs display a catalytic efficiency comparable to that of characterized bacterial Nudix ADPRPs [35], [36]. In addition, both types of ADPRPs exhibit a peculiar tendency to occur in a fused form with enzymes involved in the recycling to NAD of its by-products, suggesting a common functional connection with NAD regeneration (Figure 1).…”
Section: Discussionmentioning
confidence: 99%
“…A high concentration of ADP-ribose in the cell causes nonenzymatic ADPribosylation, which inactivates various proteins and interferes with metabolic regulation via enzymatic ADPribosylation [55,56]. The ADP-ribose pyrophosphatases (ADPRases), which constitute a subfamily of the Nudix hydrolases, hydrolyze ADP-ribose to AMP and ribose- 5-phosphate.…”
Section: Mutations Affecting Genes Related To Degradationmentioning
confidence: 99%