Untitled

Uitdehaag, Joost C.M.; Mosi, Renée; Kalk, Kor H.; Veen, Bart A. van der; Dijkhuizen, Lubbert; Withers, Stephen G.; Dijkstra, Bauke W.

doi:10.1038/8235

Cited by 375 publications

(222 citation statements)

References 37 publications

Supporting

Mentioning

211

Contrasting

Unclassified

Order By: Relevance

“…3(b)). Slightly less similar, but more closely related to function, is domain II's similarity to the non-catalytic C-terminal carbohydrate binding domains of cyclodextrin glucosyltransferase (CTGase or a-amylase) [28] and b-amylase [29]. The crystal structures of the C-terminal domains of both CTGase and b-amylase areas are available in complex with carbohydrate molecules.…”

Section: Discussionmentioning

confidence: 99%

“…It folds into a Ig-like Greek key b-sandwich made up of one four stranded anti-parallel sheet packed against a three-stranded mixed parallel/anti-parallel b-sheet similar to that of FnIII and pre-albumin. The closest homologue is duck carboxypeptidase GP180 domain II (PDB ID 1QMU) [27] other structurally homologous domains to the RG-lyase domain II are; cyclodextrin-glycosyltransferase (a-amylase family) (PDB ID 1CXL) [28], b-amylase (PDB ID 1B9Z) [29], glucoamylase fragment (PDB ID 1KUM) [40]. (c) Domain III, residues 337-508, folds into a jelly-roll bsandwich having one sheet of five mixed parallel/anti-parallel b-strands and a second parallel sheet of four anti-parallel b-strands.…”

Section: Conserved Residues In Polysaccharide Lyase Familymentioning

confidence: 99%

See 1 more Smart Citation

Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4*1

MCDONOUGH¹

2004

FEBS Letters

View full text Add to dashboard Cite

Rhamnogalacturonan lyase (RG-lyase) specifically recognizes and cleaves a-1,4 glycosidic bonds between L L -rhamnose and D D -galacturonic acids in the backbone of rhamno galacturonan-I, a major component of the plant cell wall polysaccharide, pectin. The three-dimensional structure of RGlyase from Aspergillus aculeatus has been determined to 1.5 A resolution representing the first known structure from polysaccharide lyase family 4 and of an enzyme with this catalytic specificity. The 508-amino acid polypeptide displays a unique arrangement of three distinct modular domains. Each domain shows structural homology to non-catalytic domains from other carbohydrate active enzymes.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Conserved Residues In Polysaccharide Lyase Familymentioning

confidence: 99%

Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4*1

MCDONOUGH¹

2004

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…6). It is situated just after His 392 and Asp 393 , which are always conserved in GH family 13 and are known to stabilize the glucosyl-enzyme intermediate (20,23). The role of these four residues (Asp 394 , Arg 446 , Arg 226 , and Arg 415 ) was investigated by site-directed mutagenesis.…”

Section: Molecular Features Possibly Involved In the Polymerizationmentioning

confidence: 99%

“…The importance of three additional residues (Asp 393 , His 187 , and His 392 ), also conserved in GH family 13 and known to assist in catalysis, has been demonstrated. As a member of GH family 13, it has been assumed that AS catalysis proceeds through an ␣-retaining mechanism involving the formation of a covalent glucosyl-enzyme intermediate (21)(22)(23). The AS structure also reveals two novel domains of unknown function: an N-terminal helical domain and a BЈ-domain corresponding to an extended loop between ␤-strand 7 and ␣-helix 7 of the barrel.…”

mentioning

confidence: 99%

Molecular Basis of the Amylose-like Polymer Formation Catalyzed by Neisseria polysaccharea Amylosucrase

Albenne

Skov

Mirza

et al. 2004

Journal of Biological Chemistry

Self Cite

104

114

View full text Add to dashboard Cite

Amylosucrase from Neisseria polysaccharea is a remarkable transglucosidase from family 13 of the glycoside-hydrolases that synthesizes an insoluble amyloselike polymer from sucrose in the absence of any primer. Amylosucrase shares strong structural similarities with ␣-amylases. Exactly how this enzyme catalyzes the formation of ␣-1,4-glucan and which structural features are involved in this unique functionality existing in family 13 are important questions still not fully answered. Here, we provide evidence that amylosucrase initializes polymer formation by releasing, through sucrose hydrolysis, a glucose molecule that is subsequently used as the first acceptor molecule. Maltooligosaccharides of increasing size were produced and successively elongated at their nonreducing ends until they reached a critical size and concentration, causing precipitation. The ability of amylosucrase to bind and to elongate maltooligosaccharides is notably due to the presence of key residues at the OB1 acceptor binding site that contribute strongly to the guidance (Arg 415 , subsite ؉4) and the correct positioning (Asp 394 and Arg 446 , subsite ؉1) of acceptor molecules. On the other hand, Arg 226 (subsites ؉2/؉3) limits the binding of maltooligosaccharides, resulting in the accumulation of small products (G to G3) in the medium. A remarkable mutant (R226A), activated by the products it forms, was generated. It yields twice as much insoluble glucan as the wild-type enzyme and leads to the production of lower quantities of by-products.Amylosucrase (EC 2.4.1.4) is a glucansucrase belonging to glycoside-hydrolase (GH) 1 family 13 (1, 2). 2 This transglucosidase catalyzes the synthesis of an insoluble amylose-like polymer from sucrose (3), a cheap and easily available agroresource. This is in contrast to starch or glycogen synthases (4), which require nucleotide-activated sugar as a donor. Amylosucrase is thus attractive for the industrial synthesis of amyloselike polymers and for the modification of glucans (in particular to form nondigestible glucans) (5). Remarkably, amylosucrase is the only member of GH family 13 displaying polymerase activity and is clearly unique in this family that mainly contains starch-degrading enzymes. Amylosucrase was first isolated in the culture supernatant of Neisseria perflava (3) and later identified in various Neisseria strains (6, 7). Recently, data mining has revealed the presence of genes encoding putative amylosucrases in the genome of many other organisms such as Deinococcus radiodurans (8), Caulobacter crescentus (9), Xanthomonas campestris, Xanthomonas axonopodis (10), and Pirellula sp. (11). Recombinant amylosucrase from Neisseria polysaccharea (AS) has been the most extensively studied amylosucrase. The gene encoding AS (1) has been cloned, and its product has been purified to homogeneity. Characterization of the reaction products synthesized from sucrose substrate showed that sucrose isomers (turanose and trehalulose), glucose, maltose, and maltotriose were also produced besides the insoluble...

show abstract

“…During normal catalysis, this oxazolinium ion intermediate is formed by nucleophilic attack of the N-acetyl group of the Ϫ1 sugar on the anomeric carbon, which occurs concomitantly with protonation and breakage of the scissile glycosidic bond by the catalytic acid (refs. 17-21; note that this ''substrate-assisted'' retaining mechanism differs from the ''classical'' retaining mechanism in glycosyl hydrolases (22)(23)(24) in which a carboxylate side chain, usually a glutamic acid, is the nucleophile).…”

mentioning

confidence: 99%

High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: Mimicry of carbohydrate substrate

Houston

Shiomi

Arai

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Over the past years, family 18 chitinases have been validated as potential targets for the design of drugs against human pathogens that contain or interact with chitin during their normal life cycles. Thus far, only one potent chitinase inhibitor has been described in detail, the pseudotrisaccharide allosamidin. Recently, however, two potent natural-product cyclopentapeptide chitinase inhibitors, argifin and argadin, were reported. Here, we describe highresolution crystal structures that reveal the details of the interactions of these cyclopeptides with a family 18 chitinase. The structures are examples of complexes of a carbohydrateprocessing enzyme with high-affinity peptide-based inhibitors and show in detail how the peptide backbone and side chains mimic the interactions of the enzyme with chitooligosaccharides. Together with enzymological characterization, the structures explain why argadin shows an order of magnitude stronger inhibition than allosamidin, whereas argifin shows weaker inhibition. The peptides bind to the chitinase in remarkably different ways, which may explain the differences in inhibition constants. The two complexes provide a basis for structure-based design of potent chitinase inhibitors, accessible by standard peptide chemistry.

show abstract

Untitled

Cited by 375 publications

References 37 publications

Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4*1

Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4*1

Molecular Basis of the Amylose-like Polymer Formation Catalyzed by Neisseria polysaccharea Amylosucrase

High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: Mimicry of carbohydrate substrate

Contact Info

Product

Resources

About