Function and Tertiary- and Quaternary-structure of Cyclodextrin-hydrolyzing Enzymes (CDase), a Group of Multisubstrate Specific Enzymes Belonging to the &amp;alpha;-Amylase Family

Park, Kwan-Hwa

doi:10.5458/jag.53.35

Cited by 11 publications

(11 citation statements)

References 38 publications

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“…Thus, the maltogenic amylases constitute a special subfamily of the GH-13 or the a-amylase family together with neopullulanase, cyclomaitodextrinase, and Thermoactinomyces vulgaris R47 amylase II [11,13,14]. These enzymes share similar characteristics of maltogenic amylase [5,[15][16][17]. In general, maltogenic amylases displayed multiple activities.…”

Section: Discussionmentioning

confidence: 99%

Functional characterization of a special thermophilic multifunctional amylase OPMA-N and its N-terminal domain

Li¹,

Zhu²,

Li³

et al. 2011

ABBS

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A gene encoding a special thermophilic multifunctional amylase OPMA-N was cloned from Bacillus sp. ZW2531-1. OPMA-N has an additional 124-residue N-terminal domain compared with typical amylases and forms a relatively independent domain with a b-pleated sheet and random coil structure. Here we reported an unusual substrate and product specificities of OPMA-N and the impact of the additional N-terminal domain (1 -124 aa) on the function and properties of OPMA-N. Both OPMA-N (12.82 U/mg) and its N-terminal domain-truncated DOPMA-N (12.55 U/mg) only degraded starch to produce oligosaccharides including maltose, maltotriose, isomaltotriose, and isomaltotetraose, but not to produce glucose. Therefore, the N-terminal domain did not determine its substrate and product specificities that were probably regulated by its C-terminal b-pleated sheet structure. However, the N-terminal domain of OPMA-N seemed to modulate its catalytic feature, leading to the production of more isomaltotriose and less maltose, and it seemed to contribute to OPMA-N's thermostability since OPMA-N showed higher activity than DOPMA-N in a temperature range from 40 to 808 8 8 8 8C and the halflife (t1 2

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Section: Discussionmentioning

confidence: 99%

Functional characterization of a special thermophilic multifunctional amylase OPMA-N and its N-terminal domain

Li¹,

Zhu²,

Li³

et al. 2011

ABBS

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“…7) in the presence of substrate. (7), or without OPMA (8). Lanes 9-11 reaction product(s) from maltotriose plus maltose without OPMA (9), with inactive OPMA (10), or active OPMA (11).…”

Section: Resultsmentioning

confidence: 99%

“…Lanes 3-5 reaction product(s) from maltose with active OPMA (3), inactive OPMA (4), without OPMA (5). Lanes 6-8 reaction product(s) from maltose plus glucose with active OPMA (6), inactive OPMA (7), or without OPMA (8). b HPLC quantitative analysis of products obtained from maltose or maltose plus glucose by OPMA.…”

Section: Resultsmentioning

confidence: 99%

“…OPMA could form homodimer or homotrimer like MAase [13], CDase [14], or NPase [15]. Dimerization or oligomerization could make them provide simultaneously more than one binding site for donor and acceptor molecules in enzyme active center for transglycosylation or condensation reaction [3,4,8,[15][16][17].…”

Section: Discussionmentioning

confidence: 99%

“…OPMA catalyzed starch degradation into maltose, maltotriose, and isomaltotriose as well as small amounts of isomaltotetraose, but does not produce glucose. Apparently, OPMA is distinguished from other typical amylases, such as α-amylase or other popular multifunctional amylases such as maltogenic amylase (MAase) [3,4], neopullulanase (NPase) [5,6], or cyclodextrin-hydrolyzing enzymes (CDase) [7,8], not only by its multiple activities, but also by its product composition though they all have the catalytic versatility [9][10][11].…”

Section: Introductionmentioning

confidence: 99%

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Preliminary Investigation on the Action Modes of an Oligosaccharide-Producing Multifunctional Amylase

Wang

Zhang

2009

Appl Biochem Biotechnol

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The action modes of an oligosaccharide-producing multifunctional amylase (OPMA) were investigated using glucose and some oligosaccharides as its substrates. OPMA did not cause the hydrolysis of maltose or isomaltose, but it catalyzed the alpha-1,6-transglycosylation of maltose to produce isomaltose or did the self-condensation of isomaltose to form isomaltotetraose and 4-O-alpha-isomaltosyl isomaltose. OPMA exhibited strong alpha-1,6-transglycosylation activity in addition to its alpha-1,4-hydrolytic activity on higher oligosaccharides substrates rather than bisaccharides. OPMA displayed high acceptor specificity in its transglycosylation or condensation reaction. OPMA seemed to only take glucose or isomaltose as the acceptor molecule in its transglycosylation or condensation reaction, which made glucose or isomaltose form higher products, and as a result, glucose or isomaltose were absent in the final products. In view of the simultaneously formation of several transglycosylation or condensation products, it was predicted that there might be separate donor and acceptor sites in OPMA's active center and the fact that the catalytically active form of this enzyme included its homodimer or homotrimer supported this prediction. Accordingly, a special pathway, isomaltose pathway, for OPMA catalysis was proposed to emphasize the central or important signification of isomaltose in OPMA catalysis.

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Changes in the catalytic properties and substrate specificity of Bacillus sp. US149 maltogenic amylase by mutagenesis of residue 46

Mabrouk

Ayadi-Zouari

Hlima

et al. 2013

Journal of Industrial Microbiology and Biotechnology

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Maltogenic amylase from Bacillus sp. US149 (MAUS149) is a cyclodextrin (CD)-degrading enzyme with a high preference for CDs over maltooligosaccharides. In this study, we investigated the roles of residue Asp46 in the specificity and catalytic properties of MAUS149 by using site-directed mutagenesis. Three mutated enzymes (D46V, D46G and D46N) were constructed and studied. The three mutants were found to be similar to the wild-type MAUS149 regarding thermoactivity, thermostability and pH profile. Nevertheless, the kinetic parameters for all the substrates of the mutant enzymes D46V and D46G were altered enormously as compared with those of the wild type. Indeed, the K(m) values of MAUS149/D46G for all substrates were strongly increased. Nevertheless, the affinity and catalytic efficiency of MAUS149/D46V toward β-CD were increased fivefold as compared with those of MAUS149. Molecular modelling suggests that residue D46 forms a salt bridge with residue K282. This bond would maintain the arrangement of side chains of residues Y45 and W47 in a particular orientation that promotes access to the catalytic site and maintains the substrate therein. Hence, any replacement with uncharged amino acids influenced the flexibility of the gate wall at the substrate binding cleft resulting in changes in substrate selectivity.

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Function and Tertiary- and Quaternary-structure of Cyclodextrin-hydrolyzing Enzymes (CDase), a Group of Multisubstrate Specific Enzymes Belonging to the α-Amylase Family

Cited by 11 publications

References 38 publications

Functional characterization of a special thermophilic multifunctional amylase OPMA-N and its N-terminal domain

Functional characterization of a special thermophilic multifunctional amylase OPMA-N and its N-terminal domain

Preliminary Investigation on the Action Modes of an Oligosaccharide-Producing Multifunctional Amylase

Changes in the catalytic properties and substrate specificity of Bacillus sp. US149 maltogenic amylase by mutagenesis of residue 46

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