Abstract
| Original language | English |
|---|---|
| Title of host publication | Enzymatic degradation of insoluble carbohydrates |
| Subtitle of host publication | ACS Symposium Series |
| Editors | John N Saddler, Michael H Penner |
| Publisher | American Chemical Society |
| Pages | 59-65 |
| Volume | 618 |
| ISBN (Print) | 9780841233416 |
| State | Published - May 6 1996 |
Publication series
| Name | ACS Symposium Series |
|---|
| Name | ACS Symposium Series |
|---|---|
| Number | 5 |
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The three-dimensional structure of an endochitinase from barley : ACS Symposium Series. / Robertus, Jon D; Hart, P. John.
Enzymatic degradation of insoluble carbohydrates: ACS Symposium Series. ed. / John N Saddler; Michael H Penner. Vol. 618 American Chemical Society, 1996. p. 59-65 (ACS Symposium Series), (ACS Symposium Series; No. 5).Research output: Chapter in Book/Report/Conference proceeding › Chapter
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TY - CHAP
T1 - The three-dimensional structure of an endochitinase from barley
T2 - ACS Symposium Series
AU - Robertus, Jon D
AU - Hart, P. John
PY - 1996/5/6
Y1 - 1996/5/6
N2 - Endochitinases hydrolyze chitin, cleaving glycosidic bonds within the insoluble polymer. Chitin is extremely abundant, being found in the exoskeletons of many insects, crustacea and fungi. Chitinases are of commercial interest since they can be used to create chitin oligomers useful in the chemical, pharmaceutical, and food industries. We have determined the X-ray structure of the chitinase from barley. The model has been refined to high accuracy against 1.8 data. This chitinase has 10 α-helices comprising 47% of the structure. It has a very pronounced cleft, assumed to be the chitin binding and catalytic site. A number of residues, which are conserved within the chitinase family, cluster in this cleft. Presumably they play key roles in chitin binding and hydrolysis. Barley chitinase reveals an ancient resemblance to lysozyme; they share a common central core despite lacking any obvious amino acid sequence similarity. In barley chitinase, Glu 67 appears to act as the proton donor and Glu 89 as the general base in the catalytic mechanism.
AB - Endochitinases hydrolyze chitin, cleaving glycosidic bonds within the insoluble polymer. Chitin is extremely abundant, being found in the exoskeletons of many insects, crustacea and fungi. Chitinases are of commercial interest since they can be used to create chitin oligomers useful in the chemical, pharmaceutical, and food industries. We have determined the X-ray structure of the chitinase from barley. The model has been refined to high accuracy against 1.8 data. This chitinase has 10 α-helices comprising 47% of the structure. It has a very pronounced cleft, assumed to be the chitin binding and catalytic site. A number of residues, which are conserved within the chitinase family, cluster in this cleft. Presumably they play key roles in chitin binding and hydrolysis. Barley chitinase reveals an ancient resemblance to lysozyme; they share a common central core despite lacking any obvious amino acid sequence similarity. In barley chitinase, Glu 67 appears to act as the proton donor and Glu 89 as the general base in the catalytic mechanism.
M3 - Chapter
SN - 9780841233416
VL - 618
T3 - ACS Symposium Series
SP - 59
EP - 65
BT - Enzymatic degradation of insoluble carbohydrates
A2 - Saddler, John N
A2 - Penner, Michael H
PB - American Chemical Society
ER -