Characterization of Amylolytic Enzymes, Having Both α-1,4 and α-1,6 Hydrolytic Activity, from the Thermophilic Archaea
            <i>Pyrococcus furiosus</i>
            and
            <i>Thermococcus litoralis</i>

Brown, Stephen H.M.; Kelly, Robert M.

doi:10.1128/aem.59.8.2614-2621.1993

Cited by 154 publications

(40 citation statements)

References 36 publications

(28 reference statements)

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“…strain EM1 (now Thermoanaerobacterium thermosulfurogenes), 37,38 Thermoanaerobium brockii, 10 Thermoanaerobium Tok6-B1, 40,41 Thermoanaerobacterium thermosaccharolyticum, 42 Thermoanaerobacter ethanolicus 39E, 43 Thermoanaerobacter finni, 44,45 Thermobacteroides acetoethylicus, 44,45 T. ethanolicus, 44,45 Thermotoga maritime, 46 and Thermococcus profundus 47 are identified as producers of amylopullulanase. The GH57 family amylopullulanases 2 have been produced from archaea Pyrococcus furiosus, 48 P. woesei, 49 Thermococcus litoralis, 50 T. celer, 51 T. hydrothermalis, 52,53 and T. siculi. 19…”

Section: Microorganisms Producing Amylopullulanasesmentioning

confidence: 99%

Recombinant bacterial amylopullulanases

Mohanan

Satyanarayana

2013

Bioengineered

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Pullulanases are endo-acting enzymes capable of hydrolyzing α-1, 6-glycosidic linkages in starch, pullulan, amylopectin, and related oligosaccharides, while amylopullulanases are bifunctional enzymes with an active site capable of cleaving both α-1, 4 and α-1, 6 linkages in starch, amylose and other oligosaccharides, and α-1, 6 linkages in pullulan. The amylopullulanases are classified in GH13 and GH57 family enzymes based on the architecture of catalytic domain and number of conserved sequences. The enzymes with two active sites, one for the hydrolysis of α-1, 4- glycosidic bond and the other for α-1, 6-glycosidic bond, are called α-amylase-pullulanases, while amylopullulanases have only one active site for cleaving both α-1, 4- and α-1, 6-glycosidic bonds. The amylopullulanases produced by bacteria find applications in the starch and baking industries as a catalyst for one step starch liquefaction-saccharification for making various sugar syrups, as antistaling agent in bread and as a detergent additive.

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Section: Microorganisms Producing Amylopullulanasesmentioning

confidence: 99%

Recombinant bacterial amylopullulanases

Mohanan

Satyanarayana

2013

Bioengineered

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“…The pullulan-hydrolysing enzymes isolated from other extreme thermophiles are all amylopullulanases, i.e. enzymes that cleave K-1,6-glucosidic bonds in pullulan but also K-1,4bonds in starch [2,7].…”

Section: Pullulanasementioning

confidence: 99%

Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima

Bibel

1998

FEMS Microbiology Letters

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In addition to the previously identified 4-K-glucanotransferase gene mgtA and the K-amylase gene amyA of Thermotoga maritima strain MSB8 we have now isolated three further genes encoding amylolytic enzymes from a gene library of this ancestral bacterium. The genes code for the extremely thermostable enzymes pullulanase (pulA), maltodextrin phosphorylase (agpA) and K-glucosidase (aglA) and have the potential to encode polypeptides with calculated molecular masses of 96.3 kDa, 96.1 kDa and 52.5 kDa, respectively. Comparative amino acid sequence analysis revealed that PulA and AgpA are clearly related to other known enzymes with similar function. AglA, on the other hand, was not related to other K-glucosidases but appears to belong to an enzyme family containing K-galactosidases and 6-phospho-L-glucosidases. Enzyme properties are reported which demonstrate the extreme thermostability of these T. maritima enzymes. ß

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“…Pyrococcus sp. produce both amylases and glucosidases to hydrolyze starch and its degradation products to glucose [23][24][25][26][27]. These carbohydrate-metabolizing enzymes are among the most thermostable proteins currently known.…”

Section: Carbohydrate Metabolism In P Furiosusmentioning

confidence: 99%

Biochemical diversity among sulfur-dependent, hyperthermophilic microorganisms

Adams

1994

FEMS Microbiology Reviews

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Hyperthermophiles are a recently discovered group of microorganisms that grow at and above 90 degrees C. They currently comprise over 20 different genera, and except for two novel bacteria, all are classified as Archaea. The majority of these organisms are obligately anaerobic heterotrophs that reduce elemental sulfur (S degree) to H2S. The best studied from a biochemical perspective are the archaeon, Pyrococcus furiosus, and the bacterium, Thermotoga maritima, both of which are saccharolytic. P. furiosus is thought to contain a new type of Entner-Doudoroff pathway for the conversion of carbohydrates ultimately to acetate, H2 and CO2. The pathway is independent of nicotinamide nucleotides and involves novel types of ferredoxin-linked oxidoreductases, one of which has tungsten, a rarely used element, as a prosthetic group. The only site of energy conservation is at the level of acetyl CoA, which is the presence of ADP and phosphate is converted to acetate and ATP in a single step. In contrast, T. maritima utilizes a conventional Embden-Meyerhof pathway for sugar oxidation. P. furiosus also utilizes peptides as a sole carbon and energy source. Amino acid oxidation is thought to involve glutamate dehydrogenase together with at least three types of novel ferredoxin-linked oxidoreductases which catalyze the oxidation of 2-ketoglutarate, aryl pyruvates and formaldehyde. One of these enzymes also utilizes tungsten. In P. furiosus, virtually all of the reductant that is generated during the catabolism of both carbohydrates and peptides is channeled to a cytoplasmic hydrogenase. This enzyme is now termed sulhydrogenase, as it reduces both protons to H2 and S degrees (or polysulfide) to H2S. S degrees reduction appears to lead to the conservation of energy in P. furiosus but not in T. maritima, although the mechanism by which this occurs is not known.

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Characterization of Amylolytic Enzymes, Having Both α-1,4 and α-1,6 Hydrolytic Activity, from the Thermophilic Archaea Pyrococcus furiosus and Thermococcus litoralis

Cited by 154 publications

References 36 publications

Recombinant bacterial amylopullulanases

Recombinant bacterial amylopullulanases

Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima

Biochemical diversity among sulfur-dependent, hyperthermophilic microorganisms

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