The activity of barley α-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase

Juge, Nathalie; Nøhr, Jane; Gal-Coeffet, M.-F. Le; Kramhøft, Birte; Furniss, Caroline S.M.; Planchot, Véronique; Archer, David B.; Williamson, Gary; Svensson, Birte

doi:10.1016/j.bbapap.2005.11.008

Cited by 43 publications

(38 citation statements)

References 58 publications

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“…In this respect, the fusion of AMY-1 with an SBD increases DMA (Kramhøft et al 2005;Juge et al 2006). Likewise, the high DMA-values for the maltogenic BStA and PPA (Bijttebier et al, 2007a) are in agreement with the importance of such starch interaction sites in determining DMA.…”

Section: Mechanism Of Multiple Attacksupporting

confidence: 70%

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Amylase action pattern on starch polymers

2008

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Several decades ago, the first reports on differences in action pattern between amylases from different sources indicated that the starch polymers are not degraded in a completely random manner. We here give an overview of different action patterns of amylases on amylose and amylopectin, focusing on the so-called multiple attack action of the enzymes. Nowadays, the multiple attack action is generally an accepted concept to explain the differences in amylase action pattern. However, the pancreatic α-amylase remains one of the few enzymes known with a considerable level of multiple attack action. Despite some recent studies, the molecular mechanism of the multiple attack action is still largely unclear. Probably, the degree to which the active site architecture and binding properties allow both the reorganization (sliding) of the substrate in the active site and the stabilisation of the productive enzyme/substrate complex mainly determine the multiple attack action of amylases.

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Section: Mechanism Of Multiple Attacksupporting

confidence: 70%

“…Many amylases possess additional domains, such as a starch binding domain (SBD). This is almost exclusively positioned at the C-terminal part of the amylase (Janecek & Sevcik 1999) and makes it possible for the amylase to bind and hydrolyse native granular starch (Juge et al 2006). It functions independently of the amylase.…”

Section: Classificationmentioning

confidence: 99%

Amylase action pattern on starch polymers

2008

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“…A variety of CBMs representing an array of polysaccharide specificities have been identified (http://www.cazy.org/). These are widely used in studies of heterogeneous catalytic degradation of insoluble substrates as well as in applications taking advantage of the CBM affinity to direct enzyme-CBM fusion proteins to the surface of the substrate in question (Juge et al 2006). In addition to the first identified SBD (CBM20), 7 CBM families of SBDs have been reported (Boraston et al 2004(Boraston et al , 2006Machovic & Janecek 2006.…”

Section: Binding To Starchesmentioning

confidence: 99%

An enzyme family reunion — similarities, differences and eccentricities in actions on α-glucans

et al. 2008

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α-Glucans in general, including starch, glycogen and their derived oligosaccharides are processed by a host of more or less closely related enzymes that represent wide diversity in structure, mechanism, specificity and biological role. Sophisticated three-dimensional structures continue to emerge hand-in-hand with the gaining of novel insight in modes of action. We are witnessing the "test of time" blending with remaining questions and new relationships for these enzymes. Information from both within and outside of ALAMY 3 Symposium will provide examples on what the family contains and outline some future directions. In 2007 a quantum leap crowned the structural biology by the glucansucrase crystal structure. This initiates the disclosure of the mystery on the organisation of the multidomain structure and the "robotics mechanism" of this group of enzymes. The central issue on architecture and domain interplay in multidomain enzymes is also relevant in connection with the recent focus on carbohydrate-binding domains as well as on surface binding sites and their long underrated potential. Other questions include, how different or similar are glycoside hydrolase families 13 and 31 and is the lid finally lifted off the disguise of the starch lyase, also belonging to family 31? Is family 57 holding back secret specificities? Will the different families be sporting new "eccentric" functions, are there new families out there, and why are crystal structures of "simple" enzymes still missing? Indeed new understanding and discovery of biological roles continuously emphasize value of the collections of enzyme models, sequences, and evolutionary trees which will also be enabling advancement in design for useful and novel applications.

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“…Since SBD are domains which retain their structural fold and functional properties independently of the remaining parts of the protein molecule including the catalytic domain, they can be applied in various fields of biotechnology [48,[83][84][85][86]. It is important to note that most of the applications have involved only the CBM20 SBD.…”

Section: Use Of Carbohydrate-binding Modules To Change Amylose -Amylomentioning

confidence: 99%