Enzymatic preparation of maltohexaose, maltoheptaose, and maltooctaose by the preferential cyclomaltooligosaccharide (cyclodextrin) ring-opening reaction of Pyrococcus furiosus thermostable amylase

Yang, Soo Jin; Lee, Hee-Seob; Kim, Jung-Woo; Lee, Myoung-Hee; Auh, Joong-Hyuck; Lee, Byong-Hoon; Park, Kwan-Hwa

doi:10.1016/j.carres.2005.11.031

Cited by 24 publications

(13 citation statements)

References 10 publications

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“…4). The same result was obtained in our previous experiments (33). In contrast, TA(D440H) and TA(M439W/D440H) liberated various small maltooligosaccharides from the CDs (Fig.…”

Section: Vol 73 2007 Change In the Catalytic Properties Of P Furiosupporting

confidence: 89%

“…Of the archaeal enzymes, Pyrococcus furiosus thermostable amylase (TA) has a distinguishable substrate preference for cyclic maltodextrins over linear maltooligosaccharides (34). Its unique catalytic properties are useful for producing high-value-added maltooligosaccharides with defined lengths, such as maltohexaose (G6), maltoheptaose (G7), and maltooctaose (G8), from commercially available ␣-, ␤-, and ␥-CDs, respectively (33).…”

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confidence: 99%

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Changes in the Catalytic Properties of Pyrococcus furiosus Thermostable Amylase by Mutagenesis of the Substrate Binding Sites

Yang

Min²,

Kim

et al. 2007

Appl Environ Microbiol

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Pyrococcus furiosus thermostable amylase (TA) is a cyclodextrin (CD)-degrading enzyme with a high preference for CDs over maltooligosaccharides. In this study, we investigated the roles of four residues (His414, Gly415, Met439, and Asp440) in the function of P. furiosus TA by using site-directed mutagenesis and kinetic analysis. A variant form of P. furiosus TA containing two mutations (H414N and G415E) exhibited strongly enhanced ␣-(1,4)-transglycosylation activity, resulting in the production of a series of maltooligosaccharides that were longer than the initial substrates. In contrast, the variant enzymes with single mutations (H414N or G415E) showed a substrate preference similar to that of the wild-type enzyme. Other mutations (M439W and D440H) reversed the substrate preference of P. furiosus TA from CDs to maltooligosaccharides. Relative substrate preferences for maltoheptaose over ␤-CD, calculated by comparing k cat /K m ratios, of 1, 8, and 26 for wild-type P. furiosus TA, P. furiosus TA with D440H, and P. furiosus TA with M439W and D440H, respectively, were found. Our results suggest that His414, Gly415, Met439, and Asp440 play important roles in substrate recognition and transglycosylation. Therefore, this study provides information useful in engineering glycoside hydrolase family 13 enzymes.

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“…4). The same result was obtained in our previous experiments (33). In contrast, TA(D440H) and TA(M439W/D440H) liberated various small maltooligosaccharides from the CDs (Fig.…”

Section: Vol 73 2007 Change In the Catalytic Properties Of P Furiosupporting

confidence: 89%

mentioning

confidence: 99%

Changes in the Catalytic Properties of Pyrococcus furiosus Thermostable Amylase by Mutagenesis of the Substrate Binding Sites

Yang

Min²,

Kim

et al. 2007

Appl Environ Microbiol

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“…For A. fulgidus, the in vivo function of the enzyme in starch degradation was concluded from its induction after growth on starch. A. fulgidus CDase catalyzes exclusively the ring opening of cyclodextrins to the respective maltooligodextrins the rather than their further degradation to maltose and glucose, which is a typical feature of all other CDases (11,20,50,73). The enzyme showed the highest catalytic efficiency for ␥-cyclodextrin as a substrate, as described for CDase from K. oxytoca (13).…”

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confidence: 74%

“…Many CDases are described for the bacteria Bacillaceae and Enterobacteriaceae (50), whereas from the domain of Archaea, only two CDases from Thermococcus sp. strain B1001 and from P. furiosus have been characterized as recombinant enzymes (20,73). For A. fulgidus, the in vivo function of the enzyme in starch degradation was concluded from its induction after growth on starch.…”

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confidence: 99%

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

Labes

Schönheit

2007

J Bacteriol

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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, ␣-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 ␤-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.

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“…Dimaltotetraosyl-␤-cyclodextrin [(Glc 4 ) 2 -␤-CD] was prepared by a modification of the method of Kang et al (26). To prepare maltotetraosyl-␣-1,6 maltoheptaose, Glc 4 -␤-CD was hydrolyzed with Pyrococcus furiosus amylase (PfTA), and the product was purified on a butyl-Sepharose column (27).…”

Section: Methodsmentioning

confidence: 99%

Reaction Kinetics of Substrate Transglycosylation Catalyzed by TreX of Sulfolobus solfataricus and Effects on Glycogen Breakdown

Nguyen

Park

Shim

et al. 2014

Journal of Bacteriology

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Enzymatic preparation of maltohexaose, maltoheptaose, and maltooctaose by the preferential cyclomaltooligosaccharide (cyclodextrin) ring-opening reaction of Pyrococcus furiosus thermostable amylase

Cited by 24 publications

References 10 publications

Changes in the Catalytic Properties of Pyrococcus furiosus Thermostable Amylase by Mutagenesis of the Substrate Binding Sites

Changes in the Catalytic Properties of Pyrococcus furiosus Thermostable Amylase by Mutagenesis of the Substrate Binding Sites

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

Reaction Kinetics of Substrate Transglycosylation Catalyzed by TreX of Sulfolobus solfataricus and Effects on Glycogen Breakdown

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