The 1.8 Å Resolution Structure of Hevamine, a Plant Chitinase/Lysozyme, and Analysis of the Conserved Sequence and Structure Motifs of Glycosyl Hydrolase Family 18

Scheltinga, Anke C. Terwisscha van; Hennig, Michael; Dijkstra, Bauke W.

doi:10.1006/jmbi.1996.0510

Cited by 175 publications

(163 citation statements)

References 39 publications

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“…where Glu is the catalytic amino acid [24] characteristic of chitinase family 18 [7] and Xaa is any amino acid. This family comprises proteins from organisms as diverse as arthropods, bacteria, fungi, plants, nematodes and vertebrates.…”

Section: Figure 3 Developmental Profiles Of Tmchit5 and Tmecr Epidermmentioning

confidence: 99%

A novel putative insect chitinase with multiple catalytic domains: hormonal regulation during metamorphosis

Royer

Fraichard

Bouhin

2002

Biochemical Journal

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We have used differential display to identify genes that are regulated by juvenile hormone in the epidermis of the beetle Tenebrio molitor. One of the genes encodes T. molitor chitinase 5 (TmChit5), a chitinase possessing an unusual structure. Sequence analysis of TmChit5 identified five ' chitinase units ' of approx. 480 amino acids with similarity to chitinase family 18. These units are separated by less conserved regions containing putative PEST (rich in proline, glutamic acid, serine and threonine) sequences, putative chitin-binding domains and mucin domains. Northern-blot analysis identified a single transcript of approx. 9 kb, whose abundance correlated with that of

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Section: Figure 3 Developmental Profiles Of Tmchit5 and Tmecr Epidermmentioning

confidence: 99%

A novel putative insect chitinase with multiple catalytic domains: hormonal regulation during metamorphosis

Royer

Fraichard

Bouhin

2002

Biochemical Journal

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“…These aromatic residues are conserved between hCHT, YKL-40 and YKL-39, except for a single tryptophan-to-tyrosine substitution in YKL-39 (Tyr 104 in Figures 1B and 2). Stacking between sugar ligands and tryptophans in their cognate binding proteins/enzymes is known to be an important contribution to binding affinity in proteinglycan complexes [33,45,46]. Previous mutational studies of the conserved tryptophans in active chitinases have shown a reduction or complete loss of activity [45,47,48].…”

Section: Ykl-39 Adopts a Chitinase-like Fold But Does Not Possess A Cmentioning

confidence: 99%

“…The active site motif DxxDxDxE, essential for the activity of GH18 chitinases [31,33,34], is not conserved in YKL-39 ( Figure 1B). Catalysis involves participation of the acetamido group of N-acetylglucosamine and proceeds via a bicyclic oxazoline intermediate [31,33,44]. The last aspartate residue in the DxxDxDxE motif (Asp 138 in hCHT) positions the acetamido group for nucleophilic attack, whereas the glutamate residue (Glu 140 ) performs general acid/base catalysis ( Figure 2E).…”

Section: Ykl-39 Adopts a Chitinase-like Fold But Does Not Possess A Cmentioning

confidence: 99%

“…The loss of enzymatic activity is attributed to the substitution of the catalytic residues of the DxxDxDxE motif, which characterizes the active site of family 18 chitinases [13,[31][32][33][34]. Although YKL-39 appears to have an active site incompatible with chitin hydrolysis, it may have retained the ability to bind chitin-like molecules, although the identity of the physiological ligand, if any, is currently unknown.…”

Section: Introductionmentioning

confidence: 99%

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Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide-binding properties

Schimpl

Rush

Betou

et al. 2012

Biochemical Journal

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The chitinase-like proteins YKL-39 (chitinase 3-like-2) and YKL-40 (chitinase 3-like-1) are highly expressed in a number of human cells independent of their origin (mesenchymal, epithelial or haemapoietic). Elevated serum levels of YKL-40 have been associated with a negative outcome in a number of diseases ranging from cancer to inflammation and asthma. YKL-39 expression has been associated with osteoarthritis. However, despite the reported association with disease, the physiological or pathological role of these proteins is still very poorly understood. Although YKL-39 is homologous to the two family 18 chitinases in the human genome, it has been reported to lack any chitinase activity. In the present study, we show that human YKL-39 possesses a chitinase-like fold, but lacks key active-site residues required for catalysis. A glycan screen identified oligomers of N-acetylglucosamine as preferred binding partners. YKL-39 binds chitooligosaccharides and a newly synthesized derivative of the bisdionin chitinase-inhibitor class with micromolar affinity, through a number of conserved tryptophan residues. Strikingly, the chitinase activity of YKL-39 was recovered by reverting two non-conservative substitutions in the active site to those found in the active enzymes, suggesting that YKL-39 is a pseudo-chitinase with retention of chitinase-like ligand-binding properties.

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“…The catalytic domains of family 18 chitinases have ( / ) 8 -barrel folds and are characterized by several conserved sequence motifs (Terwisscha van Scheltinga et al, 1996;Suzuki et al, 1999). Threedimensional structures have been reported for bacterial family 18 chitinases, such as chitinases A and B from Serratia marcescens and chitinase A1 from Bacillus circulans (Perrakis et al, 1994;van Aalten et al, 2000;Matsumoto et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Structure of the catalytic domain of the hyperthermophilic chitinase fromPyrococcus furiosus

et al. 2006

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PDB Reference: archaeal chitinase, 2dsk, r2dsksf.The crystal structure of the catalytic domain of a chitinase from the hyperthermophilic archaeon Pyrococcus furiosus (AD2 PF-ChiA ) has been determined at 1.5 Å resolution. This is the first structure of the catalytic domain of an archaeal chitinase. The overall structure of AD2 PF-ChiA is a TIM-barrel fold with a tunnel-like active site that is a common feature of family 18 chitinases. Although the catalytic residues (Asp522, Asp524 and Glu526) are conserved, comparison of the conserved residues and structures with those of other homologous chitinases indicates that the catalytic mechanism of PF-ChiA is different from that of family 18 chitinases.

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The 1.8 Å Resolution Structure of Hevamine, a Plant Chitinase/Lysozyme, and Analysis of the Conserved Sequence and Structure Motifs of Glycosyl Hydrolase Family 18

Cited by 175 publications

References 39 publications

A novel putative insect chitinase with multiple catalytic domains: hormonal regulation during metamorphosis

A novel putative insect chitinase with multiple catalytic domains: hormonal regulation during metamorphosis

Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide-binding properties

Structure of the catalytic domain of the hyperthermophilic chitinase fromPyrococcus furiosus

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