Sugar utilization in the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324: starch degradation to acetate and CO 2 via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)

2001 ◽  
Vol 176 (5) ◽  
pp. 329-338 ◽  
Author(s):  
Antje Labes ◽  
Peter Schönheit
Keyword(s):  
Archaeoglobus Fulgidus ◽  
Starch Degradation ◽  
Acetyl Coa ◽  
Sugar Utilization ◽  
Sulfate Reducing ◽  
Archaeoglobus Fulgidus Strain 7324 ◽  
Modified Embden Meyerhof Pathway

scholarly journals Unusual Starch Degradation Pathway via Cyclodextrins in the Hyperthermophilic Sulfate-Reducing Archaeon Archaeoglobus fulgidus Strain 7324

2007 ◽  
Vol 189 (24) ◽  
pp. 8901-8913 ◽  
Author(s):  
Antje Labes ◽  
Peter Schönheit
Keyword(s):  
Degradation Pathway ◽  
Archaeoglobus Fulgidus ◽  
Starch Degradation ◽  
Cyclodextrin Glucanotransferase ◽  
Gene Encoding ◽  
Thermococcus Litoralis ◽  
Sulfate Reducing ◽  
Combined Action ◽  
Archaeoglobus Fulgidus Strain 7324 ◽  
Modified Embden Meyerhof Pathway

ABSTRACT The hyperthermophilic archaeon Archaeoglobus fulgidus strain 7324 has been shown to grow on starch and sulfate and thus represents the first sulfate reducer able to degrade polymeric sugars. The enzymes involved in starch degradation to glucose 6-phosphate were studied. In extracts of starch-grown cells the activities of the classical starch degradation enzymes, α-amylase and amylopullulanase, could not be detected. Instead, evidence is presented here that A. fulgidus utilizes an unusual pathway of starch degradation involving cyclodextrins as intermediates. The pathway comprises the combined action of an extracellular cyclodextrin glucanotransferase (CGTase) converting starch to cyclodextrins and the intracellular conversion of cyclodextrins to glucose 6-phosphate via cyclodextrinase (CDase), maltodextrin phosphorylase (Mal-P), and phosphoglucomutase (PGM). These enzymes, which are all induced after growth on starch, were characterized. CGTase catalyzed the conversion of starch to mainly β-cyclodextrin. The gene encoding CGTase was cloned and sequenced and showed highest similarity to a glucanotransferase from Thermococcus litoralis. After transport of the cyclodextrins into the cell by a transport system to be defined, these molecules are linearized via a CDase, catalyzing exclusively the ring opening of the cyclodextrins to the respective maltooligodextrins. These are degraded by a Mal-P to glucose 1-phosphate. Finally, PGM catalyzes the conversion of glucose 1-phosphate to glucose 6-phosphate, which is further degraded to pyruvate via the modified Embden-Meyerhof pathway.

scholarly journals Thermococcus bergensis sp. nov., a Novel Hyperthermophilic Starch-Degrading Archaeon

Biology ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 387
Author(s):  
Nils-Kåre Birkeland ◽  
Boyke Bunk ◽  
Cathrin Spröer ◽  
Hans-Peter Klenk ◽  
Peter Schönheit
Keyword(s):  
Novel Species ◽  
Hot Water ◽  
Archaeoglobus Fulgidus ◽  
Rrna Gene ◽  
Oil Reservoir ◽  
Sulfate Reducing ◽  
Sugar Degradation ◽  
Distinct Lineage ◽  
Archaeoglobus Fulgidus Strain 7324 ◽  
The 16S Rrna Gene

A novel hyperthermophilic archaeon, termed strain T7324T, was isolated from a mixed sulfate-reducing consortium recovered from hot water produced from a deep North Sea oil reservoir. The isolate is a strict anaerobic chemo-organotroph able to utilize yeast extract or starch as a carbon source. The genes for a number of sugar degradation enzymes and glutamate dehydrogenase previously attributed to the sulfate reducing strain of the consortium (Archaeoglobus fulgidus strain 7324) were identified in the nearly completed genome sequence. Sequence analysis of the 16S rRNA gene placed the strain in the Thermococcus genus, but with an average nucleotide identity that is less than 90% to its closest relatives. Phylogenomic treeing reconstructions placed the strain on a distinct lineage clearly separated from other Thermococcus spp. The results indicate that the strain T7324T represents a novel species, for which the name Thermococcus bergensis sp. nov. is proposed. The type strain is T7324T (=DSM 27149T = KCTC 15808T).

scholarly journals AMP-forming acetyl-CoA synthetases in Archaea show unexpected diversity in substrate utilization

Archaea ◽  
2006 ◽  
Vol 2 (2) ◽  
pp. 95-107 ◽  
Author(s):  
Cheryl Ingram-Smith ◽  
Kerry S. Smith
Keyword(s):  
Phylogenetic Analysis ◽  
Molecular Basis ◽  
Catalytic Efficiency ◽  
Adenosine Monophosphate ◽  
Archaeoglobus Fulgidus ◽  
Acetyl Coa ◽  
Chain Acyl ◽  
Key Enzyme ◽  
Methanothermobacter Thermautotrophicus ◽  
Branched Chain

Adenosine monophosphate (AMP)-forming acetyl-CoA synthetase (ACS; acetate:CoA ligase (AMP-forming), EC 6.2.1.1) is a key enzyme for conversion of acetate to acetyl-CoA, an essential intermediate at the junction of anabolic and catabolic pathways. Phylogenetic analysis of putative short and medium chain acyl-CoA synthetase sequences indicates that the ACSs form a distinct clade from other acyl-CoA synthetases. Within this clade, the archaeal ACSs are not monophyletic and fall into three groups composed of both bacterial and archaeal sequences. Kinetic analysis of two archaeal enzymes, an ACS fromMethanothermobacter thermautotrophicus(designated as MT-ACS1) and an ACS fromArchaeoglobus fulgidus(designated as AF-ACS2), revealed that these enzymes have very different properties. MT-ACS1 has nearly 11-fold higher affinity and 14-fold higher catalytic efficiency with acetate than with propionate, a property shared by most ACSs. However, AF-ACS2 has only 2.3-fold higher affinity and catalytic efficiency with acetate than with propionate. This enzyme has an affinity for propionate that is almost identical to that of MT-ACS1 for acetate and nearly tenfold higher than the affinity of MT-ACS1 for propionate. Furthermore, MT-ACS1 is limited to acetate and propionate as acyl substrates, whereas AF-ACS2 can also utilize longer straight and branched chain acyl substrates. Phylogenetic analysis, sequence alignment and structural modeling suggest a molecular basis for the altered substrate preference and expanded substrate range of AF-ACS2 versus MT-ACS1.

scholarly journals Novel Type of ADP-Forming Acetyl Coenzyme A Synthetase in Hyperthermophilic Archaea: Heterologous Expression and Characterization of Isoenzymes from the Sulfate Reducer Archaeoglobus fulgidus and the Methanogen Methanococcus jannaschii

2002 ◽  
Vol 184 (3) ◽  
pp. 636-644 ◽  
Author(s):  
Meike Musfeldt ◽  
Peter Schönheit
Keyword(s):  
Coenzyme A ◽  
Pyrococcus Furiosus ◽  
Sequence Similarity ◽  
Hyperthermophilic Archaea ◽  
Archaeoglobus Fulgidus ◽  
Methanococcus Jannaschii ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Α And Β Subunits

ABSTRACT Acetyl coenzyme A (CoA) synthetase (ADP forming) (ACD) represents a novel enzyme of acetate formation and energy conservation (acetyl-CoA + ADP + Pi ⇌ acetate + ATP + CoA) in Archaea and eukaryotic protists. The only characterized ACD in archaea, two isoenzymes from the hyperthermophile Pyrococcus furiosus, constitute 145-kDa heterotetramers (α2, β2). The coding genes for the α and β subunits are located at different sites in the P. furiosus chromosome. Based on significant sequence similarity of the P. furiosus genes, five open reading frames (ORFs) encoding putative ACD were identified in the genome of the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus and one ORF was identified in the hyperthermophilic methanogen Methanococcus jannaschii. The ORFs constitute fusions of the homologous P. furiosus genes encoding the α and β subunits. Two ORFs, AF1211 and AF1938, of A. fulgidus and ORF MJ0590 of M. jannaschii were cloned and functionally overexpressed in Escherichia coli. The purified recombinant proteins were characterized as distinctive isoenzymes of ACD with different substrate specificities. In contrast to the Pyrococcus ACD, the ACDs of Archaeoglobus and Methanococcus constitute homodimers of about 140 kDa composed of two identical 70-kDa subunits, which represent fusions of the homologous P. furiosus α and β subunits in an αβ (AF1211 and MJ0590) or βα (AF1938) orientation. The data indicate that A. fulgidus and M. jannaschii contains a novel type of ADP-forming acetyl-CoA synthetase in Archaea, in which the subunit polypeptides and their coding genes are fused.

scholarly journals Iron corrosion induced by the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus at 70 °C

2020 ◽  
Vol 154 ◽  
pp. 105056
Author(s):  
Oulfat Amin Ali ◽  
Emmanuel Aragon ◽  
Armand Fahs ◽  
Sylvain Davidson ◽  
Bernard Ollivier ◽  
...  
Keyword(s):  
Archaeoglobus Fulgidus ◽  
Iron Corrosion ◽  
Sulfate Reducing
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