Abstract
β-Glucosidase enzymes (EC 3.2.1-3.2.3) hydrolyze sugars and are implicated in a wide spectrum of biological processes. Recently, we reported that β-glucosidase has varied kinetic parameters for the natural and synthetic substrates [K.H Nam, S.J. Kim, M.Y. Kim, J.H. Kim, T.S. Yeo, C.M. Lee, H.K Jun, K.Y. Hwang. Crystal structure of engineered beta-glucosidase from a soil metagenome, Proteins 73 (2008) 788-793]. However, an understanding of the kinetic values of β-glucosidase has not yet enabled the elucidation of its molecular function. Here, we report the X-ray crystal structure of β-glucosidase with a glucose and cellobiose fragment from uncultured soil metagenome. From the various crystals, we obtained the pre-reaction (native), intermediate (disaccharide cleavage) and post-reaction (glucose binding) states of the active site pocket. These structures provide snapshots of the catalytic processing of β-glucosidase. In addition, the intermediate state of the crystal structure provides insight into the substrate specificity of β-glucosidase. These structural studies will facilitate elucidation of the architectural mechanism responsible for the substrate recognition of β-glucosidase.
| Original language | English |
|---|---|
| Pages (from-to) | 1131-1135 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 391 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2010 Jan 1 |
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Keywords
- β-Glucosidase
- Catalysis processing
- Intermediate state
- Steric hindrance
- Substrate specificity
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Molecular Biology
Cite this
Structural insights into the substrate recognition properties of β-glucosidase. / Nam, Ki Hyun; Sung, Min Woo; Hwang, Kwang Yeon.
In: Biochemical and Biophysical Research Communications, Vol. 391, No. 1, 01.01.2010, p. 1131-1135.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structural insights into the substrate recognition properties of β-glucosidase
AU - Nam, Ki Hyun
AU - Sung, Min Woo
AU - Hwang, Kwang Yeon
PY - 2010/1/1
Y1 - 2010/1/1
N2 - β-Glucosidase enzymes (EC 3.2.1-3.2.3) hydrolyze sugars and are implicated in a wide spectrum of biological processes. Recently, we reported that β-glucosidase has varied kinetic parameters for the natural and synthetic substrates [K.H Nam, S.J. Kim, M.Y. Kim, J.H. Kim, T.S. Yeo, C.M. Lee, H.K Jun, K.Y. Hwang. Crystal structure of engineered beta-glucosidase from a soil metagenome, Proteins 73 (2008) 788-793]. However, an understanding of the kinetic values of β-glucosidase has not yet enabled the elucidation of its molecular function. Here, we report the X-ray crystal structure of β-glucosidase with a glucose and cellobiose fragment from uncultured soil metagenome. From the various crystals, we obtained the pre-reaction (native), intermediate (disaccharide cleavage) and post-reaction (glucose binding) states of the active site pocket. These structures provide snapshots of the catalytic processing of β-glucosidase. In addition, the intermediate state of the crystal structure provides insight into the substrate specificity of β-glucosidase. These structural studies will facilitate elucidation of the architectural mechanism responsible for the substrate recognition of β-glucosidase.
AB - β-Glucosidase enzymes (EC 3.2.1-3.2.3) hydrolyze sugars and are implicated in a wide spectrum of biological processes. Recently, we reported that β-glucosidase has varied kinetic parameters for the natural and synthetic substrates [K.H Nam, S.J. Kim, M.Y. Kim, J.H. Kim, T.S. Yeo, C.M. Lee, H.K Jun, K.Y. Hwang. Crystal structure of engineered beta-glucosidase from a soil metagenome, Proteins 73 (2008) 788-793]. However, an understanding of the kinetic values of β-glucosidase has not yet enabled the elucidation of its molecular function. Here, we report the X-ray crystal structure of β-glucosidase with a glucose and cellobiose fragment from uncultured soil metagenome. From the various crystals, we obtained the pre-reaction (native), intermediate (disaccharide cleavage) and post-reaction (glucose binding) states of the active site pocket. These structures provide snapshots of the catalytic processing of β-glucosidase. In addition, the intermediate state of the crystal structure provides insight into the substrate specificity of β-glucosidase. These structural studies will facilitate elucidation of the architectural mechanism responsible for the substrate recognition of β-glucosidase.
KW - β-Glucosidase
KW - Catalysis processing
KW - Intermediate state
KW - Steric hindrance
KW - Substrate specificity
UR - http://www.scopus.com/inward/record.url?scp=72949100309&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=72949100309&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2009.12.038
DO - 10.1016/j.bbrc.2009.12.038
M3 - Article
C2 - 20005197
AN - SCOPUS:72949100309
VL - 391
SP - 1131
EP - 1135
JO - The BMJ
JF - The BMJ
SN - 0730-6512
IS - 1
ER -