Association of Novel Domain in Active Site of Archaic Hyperthermophilic Maltogenic Amylase from Staphylothermus marinus

Jung, Tae‐Yang; Li, Dan; Park, Jong-Tae; Yoon, Sei Mee; Tran, Phuong Lan; Oh, Byung‐Ha; Janeček, Štefan; Park, Sung Goo; Woo, Eui-Jeon; Park, Kwan-Hwa

doi:10.1074/jbc.m111.304774

Cited by 32 publications

(17 citation statements)

References 70 publications

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“…Moreover, the crystal structure of maltogenic amylase from Staphylothermus marinus revealed that an N‐terminal extension forms the domain N′ that together with the A and C domains constitute the substrate‐binding pocket, distinguishing the archaeal enyzme from bacterial enzymes (T.‐Y. Jung et al., ). Domains N and N′ have the same functional roles in improving the characteristics of maltogenic amylases whether from mesophilic or thermophilic organisms.…”

Section: Specific Starch‐processing Enzymesmentioning

confidence: 99%

Microbial Starch‐Converting Enzymes: Recent Insights and Perspectives

Miao

Jiang

Jin

et al. 2018

Comp Rev Food Sci Food Safe

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Starch is an abundant, natural, renewable resource, and present as the major storage carbohydrate in the seeds, roots, or tubers of many important food crops, such as maize, wheat, rice, potato, and cassava. Uses of native starches in most industrial applications are limited by their inherent properties. Hence, they are often structurally modified after isolation to enhance desirable attributes, to minimize undesirable attributes, or to create new attributes. Enzymatic, rather than chemical, approaches are used in the production of starch syrups, maltodextrins, and cyclodextrins. However, the desire for starch-active enzymes working optimally at high temperatures and low pH conditions with superior stability and activity is still not satisfied and this stimulates interest in developing novel and improved starch-active enzymes through a variety of strategies. This review provides current information on enzymes belonging to GH13, 57, 70, and 77 that can be used in structural modifications of the starch polysaccharides or to produce starch-derived products from them. The characteristics and catalytic mechanisms of microbial enzymes are discussed (including 4-α-glucanotransferase, branching enzyme, maltogenic amylase, cyclomaltodextrinase, amylosucrase, and glucansucrase). Product diversity after starch-converting reaction and utilization in industrial applications are also dealt with.

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Section: Specific Starch‐processing Enzymesmentioning

confidence: 99%

Microbial Starch‐Converting Enzymes: Recent Insights and Perspectives

Miao

Jiang

Jin

et al. 2018

Comp Rev Food Sci Food Safe

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“…This domain is also a member of the CBM48 (carbohydrate-binding module 48) family, the members of which include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme and isoamylase. In other microbial amylases, this region of the protein is referred to as the N 0domain and is involved in dimerization and the formation of a cap over the active-site cleft (Jung et al, 2012). However, gel-filtration experiments demonstrated that recombinant TK-PUL exists in a monomeric form.…”

Section: Structural Comparison With Homologuesmentioning

confidence: 99%

Structure and function of the type III pullulan hydrolase fromThermococcus kodakarensis

Guo

Coker

Wood

et al. 2018

Acta Crystallogr D Struct Biol

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Pullulan-hydrolysing enzymes, more commonly known as debranching enzymes for starch and other polysaccharides, are of great interest and have been widely used in the starch-saccharification industry. Type III pullulan hydrolase from Thermococcus kodakarensis (TK-PUL) possesses both pullulanase and α-amylase activities. Until now, only two enzymes in this class, which are capable of hydrolysing both α-1,4- and α-1,6-glycosidic bonds in pullulan to produce a mixture of maltose, panose and maltotriose, have been described. TK-PUL shows highest activity in the temperature range 95-100°C and has a pH optimum in the range 3.5-4.2. Its unique ability to hydrolyse maltotriose into maltose and glucose has not been reported for other homologous enzymes. The crystal structure of TK-PUL has been determined at a resolution of 2.8 Å and represents the first analysis of a type III pullulan hydrolyse. The structure reveals that the last part of the N-terminal domain and the C-terminal domain are significantly different from homologous structures. In addition, the loop regions at the active-site end of the central catalytic domain are quite different. The enzyme has a well defined calcium-binding site and possesses a rare vicinal disulfide bridge. The thermostability of TK-PUL and its homologues may be attributable to several factors, including the increased content of salt bridges, helical segments, Pro, Arg and Tyr residues and the decreased content of serine.

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“…and maltogenic ␣-amylase (EC 3.2.1.133) (22,40), and neopullulanase (EC 3.2.1.135) (41,42), have been reported. A database search using the DALI server (43) revealed that CMMase shows a high structural similarity to GsNPL (Z-score, 53.3; RMSD, 1.5 Å for 435 C␣ atoms), TVAII (Z-score, 53.3; RMSD, 1.3 Å for 435 C␣ atoms), ThMAA (Z-score, 52.3; RMSD, 1.6 Å for 432 C␣ atoms), and a debranching enzyme from Nostoc punctiforme (NpDBE, Z-score, 46.6; RMSD, 2.0 Å for 420 C␣ atoms).…”

Section: Overall Structure Of Cmmasementioning

confidence: 99%

Structural features of a bacterial cyclic α-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis

Kohno¹,

Arakawa

Ota

et al. 2018

Journal of Biological Chemistry

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Cyclic α-maltosyl-(1→6)-maltose (CMM, -{→6)-α-d-Glc-(1→4)-α-d-Glc-(1→6)-α-d-Glc-(1→4)-α-d-Glc-(1→})is a cyclic glucotetrasaccharide with alternating α-1,4 and α-1,6 linkages. CMM is composed of two maltose units and is one of the smallest cyclic glucooligosaccharides. Although CMM is resistant to usual amylases, it is efficiently hydrolyzed by CMM hydrolase (CMMase), belonging to subfamily 20 of glycoside hydrolase family 13 (GH13_20). Here, we determined the ligand-free crystal structure of CMMase from the soil-associated bacterium and its structures in complex with maltose, panose, and CMM to elucidate the structural basis of substrate recognition by CMMase. The structures disclosed that although the monomer structure consists of three domains commonly adopted by GH13 and other α-amylase-related enzymes, CMMase forms a unique wing-like dimer structure. The complex structure with CMM revealed four specific subsites, namely -3', -2, -1, and +1'. We also observed that the bound CMM molecule adopts a low-energy conformer compared with the X-ray structure of a single CMM crystal, also determined here. Comparison of the CMMase active site with those in other enzymes of the GH13_20 family revealed that three regions forming the wall of the cleft, denoted PYF (Pro-203/Tyr-204/Phe-205), CS (Cys-163/Ser-164), and Y (Tyr-168), are present only in CMMase and are involved in CMM recognition. Combinations of multiple substitutions in these regions markedly decreased the activity toward CMM, indicating that the specificity for this cyclic tetrasaccharide is supported by the entire shape of the pocket. In summary, our work uncovers the mechanistic basis for the highly specific interactions of CMMase with its substrate CMM.

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Association of Novel Domain in Active Site of Archaic Hyperthermophilic Maltogenic Amylase from Staphylothermus marinus

Cited by 32 publications

References 70 publications

Microbial Starch‐Converting Enzymes: Recent Insights and Perspectives

Microbial Starch‐Converting Enzymes: Recent Insights and Perspectives

Structure and function of the type III pullulan hydrolase fromThermococcus kodakarensis

Structural features of a bacterial cyclic α-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis

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