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Title 

Structural features of the Nostoc punctiforme debranching enzyme reveal the basis of its mechanism and substrate specificity

Authors 

A B DumbrepatilJ H ChoiJ T ParkM J KimEui-Jeon WooK H Park

Publisher 

Wiley-Blackwell

Issue Date 

2010

Citation 

Proteines, vol. 78, no. 2, pp. 348-356

Keywords 

Crystal structureCyclodextrin/pullulan-hydrolyzing enzymeDebranching enzymeDimerizationNeopullulanase

Abstract 

The debranching enzyme Nostoc punctiforme debranching enzyme (NPDE) from the cyanobacterium Nostoc punctiforme (PCC73102) hydrolyzes the alpha-1,6 glycosidic linkages of malto-oligosaccharides. Despite its high homology to cyclodextrin/pullulan (CD/PUL)-hydrolyzing enzymes from glycosyl hydrolase 13 family (GH-13), NPDE exhibits a unique catalytic preference for longer malto-oligosaccharides (>G8), performing hydrolysis without the transgylcosylation or CD-hydrolyzing activities of other GH-13 enzymes. To investigate the molecular basis for the property of NPDE, we determined the structure of NPDE at 2.37-A resolution. NPDE lacks the typical N-terminal domain of other CD/PUL-hydrolyzing enzymes and forms an elongated dimer in a head-to-head configuration. The unique orientation of residues 25-55 in NPDE yields an extended substrate binding groove from the catalytic center to the dimeric interface. The substrate binding groove with a lengthy cavity beyond the -1 subsite exhibits a suitable architecture for binding longer malto-oligosaccharides (>G8). These structural results may provide a molecular basis for the substrate specificity and catalytic function of this cyanobacterial enzyme, distinguishing it from the classical neopullulanases and CD/PUL-hydrolyzing enzymes.

ISSN 

0887-3585

Link 

http://dx.doi.org/10.1002/prot.22548

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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