Crystal Structure of a Maltogenic Amylase Provides Insights into a Catalytic Versatility

Kim, Jeong Sun; Shin, Sun; Kim, Hyun Ju; Kim, Tae Jip; Ha, Nam Chul; Oh, Sang Taek; Cho, Hyun Soo; Cho, Moon Ju; Kim, Myo Jeong; Lee, Hee Seob; Kim, Jung Wan; Choi, Kwan Yong; Park, Kwan Hwa; Oh, Byung Ha

doi:10.1074/jbc.274.37.26279

Cited by 157 publications

(134 citation statements)

References 29 publications

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“…Two molecules of CDase form a domain-swapped dimer in which the N-terminal domain of one molecule is involved in extensive interactions with the (␣/␤) 8 -barrel domain of the adjacent molecule (Fig. 1b), as is observed in the structure of ThMA, which is dimeric in both solution and crystals (2). In the dimeric structures, the C-terminal domain is distinctively separated from the active-site groove and is not involved in main chain-to-main chain hydrogen bonds with either the N-terminal or (␣/␤) 8 -barrel domain.…”

Section: Resultsmentioning

confidence: 96%

“…With a mutant ThMA containing the deletion of the N-terminal domain, we previously demonstrated that the domain is important for the dimerization, stability, and substrate preference of the enzyme for ␤-CD (19). We suggested that the narrow and deep activesite cleft shaped by the N-terminal domain that partly covers the otherwise wide and shallow cleft would physically restrict the easy access of the linear starch chain, whereas it allows efficient binding of CDs (1,2). Herein, we demonstrated that the N-terminal domain residue Trp 47 provides a catalytically important interaction with CDs, whereas it provides a mere interaction with soluble starch.…”

Section: Discussionmentioning

confidence: 99%

“…The vector construction resulted in the mutant enzyme fused to a His 6 tag at the N terminus. The purification and crystallization of the mutant enzyme were carried out as reported previously for the wildtype enzyme (2). E. coli BL21(DE3) cells carrying the mutant ThMA gene on the pUC119 plasmid were grown in flasks.…”

Section: Methodsmentioning

confidence: 99%

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Cyclomaltodextrinase, Neopullulanase, and Maltogenic Amylase Are Nearly Indistinguishable from Each Other

Lee¹,

Kim²,

Cho³

et al. 2002

Journal of Biological Chemistry

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147

124

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Over 20 enzymes denoted as cyclomaltodextrinase, maltogenic amylase, or neopullulanase that share 40 -86% sequence identity with each other are found in public data bases. These enzymes are distinguished from typical ␣-amylases by containing a novel N-terminal domain and exhibiting preferential substrate specificities for cyclomaltodextrins (CDs) over starch. In this research field, a great deal of confusion exists regarding the features distinguishing the three groups of enzymes from one another. Although a different enzyme code has been assigned to each of the three different enzyme names, even a single differentiating enzymatic property has not been documented in the literature. On the other hand, an outstanding question related to this issue concerns the structural basis for the preference of these enzymes for CDs. To clarify the confusion and to address this question, we have determined the structures of two enzymes, one from alkalophilic Bacillus sp. I-5 and named cyclomaltodextrinase and the other from a Thermus species and named maltogenic amylase. The structure of the Bacillus enzyme reveals a dodecameric assembly composed of six copies of the dimer, which is the structural and functional unit of the Thermus enzyme and an enzyme named neopullulanase. The structure of the Thermus enzyme in complex with ␤-CD led to the conclusion that Trp 47 , a well conserved N-terminal domain residue, contributes greatly to the preference for ␤-CD. The common dimer formation through the novel N-terminal domain, which contributes to the preference for CDs by lining the active-site cavity, convincingly indicates that the three groups of enzymes are not different enough to preserve the different names and enzyme codes.

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Section: Resultsmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

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Cyclomaltodextrinase, Neopullulanase, and Maltogenic Amylase Are Nearly Indistinguishable from Each Other

Lee¹,

Kim²,

Cho³

et al. 2002

Journal of Biological Chemistry

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147

124

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“…Similar roles for domain N have been identified in a maltogenic amylase from Thermus sp. (44), despite its role in other enzymes being unclear (37). The orientation of the cyclodextrin-GlgE interaction was close to and parallel to the linear binding cleft, near the predicted ϩ1 subsite and roughly orthogonal to the orientation of the maltose (Figs.…”

Section: Comparison Of the Catalytic And Kinetic Properties Of S Coementioning

confidence: 99%

Structure of Streptomyces Maltosyltransferase GlgE, a Homologue of a Genetically Validated Anti-tuberculosis Target

Syson

Stevenson

Rejzek

et al. 2011

Journal of Biological Chemistry

134

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Background: GlgE is a maltosyltransferase involved in bacterial ␣-glucan biosynthesis and is a genetically validated antituberculosis target. Results: We have determined the catalytic properties of Streptomyces coelicolor GlgE and solved its structure. Conclusion:The enzyme has the same catalytic properties as Mycobacterium tuberculosis GlgE and the structure reveals how GlgE functions. Significance: The structure will help guide the development of inhibitors with therapeutic potential.

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“…Three dimensional structures of various CDases including Thermus CDase, 24) TVA II from T. vulgaris, 27) and neopullulanase from B. stearothermophilus 28) were determined. The 3D structure of these enzymes gave much information for solving the questions about the unique properties of CDases.…”

Section: Tertiary and Quaternary Structure Of Cdasementioning

confidence: 99%

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

Park

2006

J. Appl. Glycosci.

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Enzymes have a long history of use in industrial applications to produce a broad range of commercial products. Many types of amylases with unique properties have been isolated and characterized for various important applications in the food and starch industry. 1,2) According to the classification system by Henrissat, 3) most of the starch hydrolyzing enzymes belong to the family 13 glycosyl hydrolases (GH13) based on amino acid sequence homology.This group of enzymes have the following features: (i) they hydrolyze glycosidic bonds of various glucans to produce anomeric mono or oligosaccharides (hydrolysis), form 1,4 or 1,6 glycosidic linkages (transglycosylation), or a combination of both activities; (ii) they possess a ( )8 barrel structure containing the catalytic site residues; (iii) they have four highly conserved regions in their primary sequence which contain the amino acids that form the catalytic site. Although these enzymes share many structural and mechanical characteristics, they can be divided into several groups according to substrate specificities, patterns of starch cleavage, transglycosylation or cyclization activities, and structural features.Jespersen et al . 4) used sequence alignments and structure prediction models to forecast the presence of amylase type ( )8 barrel domains and the positions of the strand and helices found in various amylolytic and related enzymes. An evolutionary distance tree constructed from 37 residues representing the four most highly conserved strands of these related enzymes revealed several clusters of enzymes harboring similar reaction specificities. The correlation strongly suggests that the conserved strands may determine substrate and or product specificity.Typical amylases (EC 3.2.1.1; 1,4 D glucan glucanohydrolase) catalyze the hydrolysis of 1,4 glucosidic linkages in starch and give rise to oligosaccharides with certain lengths of glucose as the major product depending on the specific enzyme.

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Crystal Structure of a Maltogenic Amylase Provides Insights into a Catalytic Versatility

Cited by 157 publications

References 29 publications

Cyclomaltodextrinase, Neopullulanase, and Maltogenic Amylase Are Nearly Indistinguishable from Each Other

Cyclomaltodextrinase, Neopullulanase, and Maltogenic Amylase Are Nearly Indistinguishable from Each Other

Structure of Streptomyces Maltosyltransferase GlgE, a Homologue of a Genetically Validated Anti-tuberculosis Target

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

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Crystal Structure of a Maltogenic Amylase Provides Insights into a Catalytic Versatility

Cited by 157 publications

References 29 publications

Cyclomaltodextrinase, Neopullulanase, and Maltogenic Amylase Are Nearly Indistinguishable from Each Other

Cyclomaltodextrinase, Neopullulanase, and Maltogenic Amylase Are Nearly Indistinguishable from Each Other

Structure of Streptomyces Maltosyltransferase GlgE, a Homologue of a Genetically Validated Anti-tuberculosis Target

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

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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