Dinucleoside Oligophosphates in Micro-organisms

Plateau, Pierre; Blanquet, Sylvain

doi:10.1016/s0065-2911(08)60177-0

Cited by 32 publications

(33 citation statements)

References 157 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although basal intracellular levels of Ap n As are 4 orders of magnitude lower than those of adenine mononucleotides, Ap n A concentrations can rise by 2 orders of magnitude under stress conditions (42,43). Also taking into consideration their extraordinarily high affinity, Ap n As could be expected to efficiently compete with mononucleotides for CBS-PPase binding in these circumstances.…”

Section: Discussionmentioning

confidence: 99%

Cystathionine β-Synthase (CBS) Domain-containing Pyrophosphatase as a Target for Diadenosine Polyphosphates in Bacteria

Anashkin

Salminen

Tuominen

et al. 2015

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Cystathionine β-Synthase (CBS) Domain-containing Pyrophosphatase as a Target for Diadenosine Polyphosphates in Bacteria

Anashkin

Salminen

Tuominen

et al. 2015

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…We could show that the enzymes exist, but their physiological role in A. ambivalens cells is unresolved. They do not play a role in the sulfur metabolism [for reviews, see Rauhut et al (1985 andPlateau andBlanquet (1994)]. Significant levels of Ap 4 A and Ap 4 A synthase activities had been found in virtually all bacteria investigated to date and in the archaeon Methanosarcina barkeri.…”

Section: Discussionmentioning

confidence: 99%

Two modes of sulfite oxidation in the extremely thermophilic and acidophilic archaeon Acidianus ambivalens

Zimmermann¹,

Laska²,

Kletzin³

1999

Archives of Microbiology

View full text Add to dashboard Cite

Sulfite-oxidizing enzyme activities were analyzed in cell-free extracts of aerobically grown cells of Acidianus ambivalens, an extremely thermophilic and chemolithoautotrophic archaeon. In the membrane and cytoplasmic fractions, two distinct enzyme activities were found. In the membrane fraction, a sulfite:acceptor oxidoreductase activity was found [530 mU (mg protein)(-1); apparent K(m) for sulfite, 3.6 mM]. In the cytoplasmic fraction the following enzyme activities were found and are indicative of an oxidative adenylylsulfate pathway: adenylylsulfate reductase [138 mU (mg protein)(-1)], adenylylsulfate:phosphate adenyltransferase ["ADP sulfurylase"; 86 mU (mg protein)(-1)], adenylate kinase [650 mU (mg protein)(-1)], and rhodanese [thiosulfate sulfur transferase, 9.2 mU (mg protein)(-1)]. In addition, 5',5"'-P(1),P(4)-di(adenosine-5') tetraphosphate (Ap(4)A) synthase and Ap(4)A pyrophosphohydrolase activities were detected.

show abstract

“…The enzyme from Bacillus stearothermophilus is also able to synthesize the hybrid polyphosphates Ap 4 G, Ap 4 U, Ap 3 U (Traut, 1987). Ap 4 A is suspected to play a regulatory role in DNA replication and cell proliferation, but these hypotheses have not been confirmed as yet (compare Plateau and Blanquet, 1994). The histidyl-adenylate bound in the active site of HisRS from B. stearothermophilus can also react with amines (Kitahata et al, 1985a), hydrazides (Kitahata, 1985b), amino acids or amino acid amides (Nakajima et al, 1984Tsuratani et al, 1986), yielding the corresponding amino acid derivatives or dipeptides.…”

Section: Mechanism Of Enzyme Actionmentioning

confidence: 99%

Histidyl-tRNA Synthetase

Freist¹,

Jf²,

Rühlmann³

et al. 1999

Biological Chemistry

View full text Add to dashboard Cite

Histidyl-tRNA synthetase (HisRS) is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. This amino acid has uniquely moderate basic properties and is an important group in many catalytic functions of enzymes.A compilation of currently known primary structures of HisRS shows that the subunits of these homodimeric enzymes consist of 420 -550 amino acid residues. This represents a relatively short chain length among aminoacyl-tRNA synthetases (aaRS), whose peptide chain sizes range from about 300 to 1100 amino acid residues.The crystal structures of HisRS from two organisms and their complexes with histidine, histidyl-adenylate and histidinol with ATP have been solved. HisRS from Escherichia coli and Thermus thermophilus are very similar dimeric enzymes consisting of three domains: the N-terminal catalytic domain containing the sixstranded antiparallel ␤-sheet and the three motifs characteristic of class II aaRS, a HisRS-specific helical domain inserted between motifs 2 and 3 that may contact the acceptor stem of the tRNA, and a C-terminal ␣/␤ domain that may be involved in the recognition of the anticodon stem and loop of tRNA His .The aminoacylation reaction follows the standard two-step mechanism. HisRS also belongs to the group of aaRS that can rapidly synthesize diadenosine tetraphosphate, a compound that is suspected to be involved in several regulatory mechanisms of cell metabolism. Many analogs of histidine have been tested for their properties as substrates or inhibitors of HisRS, leading to the elucidation of structure-activity relationships concerning configuration, importance of the carboxy and amino group, and the nature of the side chain.HisRS has been found to act as a particularly important antigen in autoimmune diseases such as rheumatic arthritis or myositis. Successful attempts have been made to identify epitopes responsible for the complexation with such auto-antibodies.

show abstract

Dinucleoside Oligophosphates in Micro-organisms

Cited by 32 publications

References 157 publications

Cystathionine β-Synthase (CBS) Domain-containing Pyrophosphatase as a Target for Diadenosine Polyphosphates in Bacteria

Cystathionine β-Synthase (CBS) Domain-containing Pyrophosphatase as a Target for Diadenosine Polyphosphates in Bacteria

Two modes of sulfite oxidation in the extremely thermophilic and acidophilic archaeon Acidianus ambivalens

Histidyl-tRNA Synthetase

Contact Info

Product

Resources

About