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Structure and function of chitinases from glycoside hydrolase family 19

Ubhayasekera, Wimal LU (2011) In Polymer International 60(6). p.890-896
Abstract
Glycoside hydrolase family 19 chitinases are found in plants, bacteria and viruses, playing various roles. Plant chitinases are important for defence and development, whereas bacterial examples are useful for nutrition. The available structural studies show that family 19 enzymes are highly alpha-helical bi-lobed structures with a wide cleft lined by conserved residues important for catalysis and substrate binding. Class I and II plant chitinases possess loops which are absent in class IV and/or bacterial chitinases. One of the loops seems to retain a significant function. These inverting endochitinases demonstrate a possible opening-closing mechanism of the catalytic cleft during chitin hydrolysis due to loop movements. However, complex... (More)
Glycoside hydrolase family 19 chitinases are found in plants, bacteria and viruses, playing various roles. Plant chitinases are important for defence and development, whereas bacterial examples are useful for nutrition. The available structural studies show that family 19 enzymes are highly alpha-helical bi-lobed structures with a wide cleft lined by conserved residues important for catalysis and substrate binding. Class I and II plant chitinases possess loops which are absent in class IV and/or bacterial chitinases. One of the loops seems to retain a significant function. These inverting endochitinases demonstrate a possible opening-closing mechanism of the catalytic cleft during chitin hydrolysis due to loop movements. However, complex structures with inhibitors and/or substrate/product analogues are required for a deeper understanding of these enzymes. (C) 2011 Society of Chemical Industry (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
endochitinase, chitinase, inverting mechanism, loop movements, opening-closing, structural studies
in
Polymer International
volume
60
issue
6
pages
890 - 896
publisher
John Wiley & Sons
external identifiers
  • wos:000291062100004
  • scopus:79956149200
ISSN
0959-8103
DOI
10.1002/pi.3028
language
English
LU publication?
yes
id
b76835e7-1fd2-4e73-b53b-9cd1f38a3f72 (old id 1985717)
date added to LUP
2011-06-27 16:05:37
date last changed
2017-08-20 03:02:58
@article{b76835e7-1fd2-4e73-b53b-9cd1f38a3f72,
  abstract     = {Glycoside hydrolase family 19 chitinases are found in plants, bacteria and viruses, playing various roles. Plant chitinases are important for defence and development, whereas bacterial examples are useful for nutrition. The available structural studies show that family 19 enzymes are highly alpha-helical bi-lobed structures with a wide cleft lined by conserved residues important for catalysis and substrate binding. Class I and II plant chitinases possess loops which are absent in class IV and/or bacterial chitinases. One of the loops seems to retain a significant function. These inverting endochitinases demonstrate a possible opening-closing mechanism of the catalytic cleft during chitin hydrolysis due to loop movements. However, complex structures with inhibitors and/or substrate/product analogues are required for a deeper understanding of these enzymes. (C) 2011 Society of Chemical Industry},
  author       = {Ubhayasekera, Wimal},
  issn         = {0959-8103},
  keyword      = {endochitinase,chitinase,inverting mechanism,loop movements,opening-closing,structural studies},
  language     = {eng},
  number       = {6},
  pages        = {890--896},
  publisher    = {John Wiley & Sons},
  series       = {Polymer International},
  title        = {Structure and function of chitinases from glycoside hydrolase family 19},
  url          = {http://dx.doi.org/10.1002/pi.3028},
  volume       = {60},
  year         = {2011},
}