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Journal of Zhejiang University SCIENCE B 2007 Vol.8 No.10 P.765~770

10.1631/jzus.2007.B0765


Identification of novel catalytic features of endo-β-1,4-glucanase produced by mulberry longicorn beetle Apriona germari


Author(s):  SAMI Amtul Jamil, HAIDER Mohammed Kamran

Affiliation(s):  Institute of Biochemistry and Biotechnology, University of the Punjab, Lahore 54594, Pakistan

Corresponding email(s):   amtuljamilsami@yahoo.com, amtul@bb.pu.edu.pk

Key Words:  Cellulases, AgEGase, Apriona germari, Inhibition, Anthocyanidins


SAMI Amtul Jamil, HAIDER Mohammed Kamran. Identification of novel catalytic features of endo-β-1,4-glucanase produced by mulberry longicorn beetle Apriona germari[J]. Journal of Zhejiang University Science B, 2007, 8(10): 765~770.

@article{title="Identification of novel catalytic features of endo-β-1,4-glucanase produced by mulberry longicorn beetle Apriona germari",
author="SAMI Amtul Jamil, HAIDER Mohammed Kamran",
journal="Journal of Zhejiang University Science B",
volume="8",
number="10",
pages="765~770",
year="2007",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.2007.B0765"
}

%0 Journal Article
%T Identification of novel catalytic features of endo-β-1,4-glucanase produced by mulberry longicorn beetle Apriona germari
%A SAMI Amtul Jamil
%A HAIDER Mohammed Kamran
%J Journal of Zhejiang University SCIENCE B
%V 8
%N 10
%P 765~770
%@ 1673-1581
%D 2007
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.2007.B0765

TY - JOUR
T1 - Identification of novel catalytic features of endo-β-1,4-glucanase produced by mulberry longicorn beetle Apriona germari
A1 - SAMI Amtul Jamil
A1 - HAIDER Mohammed Kamran
J0 - Journal of Zhejiang University Science B
VL - 8
IS - 10
SP - 765
EP - 770
%@ 1673-1581
Y1 - 2007
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.2007.B0765


Abstract: 
Mulberry longicorn beetle, Apriona germari, has been reported to produce two endo-β-1,4-glucanases or agEGases (accession Nos. Q6SS52 and Q5XQD1). agEGase sequence contains catalytic motif (amino acid residues 37~48), which is the characteristic of family Glycohydrolase 45 and is identified as the substrate binding site. The application of bioinformatics approaches includes sequence analysis, structural modeling and inhibitor docking to relate the structure and function of agEGases. We have dissected the sequence and structure of agEGase catalytic motif and compared it with crystal structure of Humicola insolens endoglucanases V. The results show an involvement of sulfur containing amino acid residues in the active site of the enzyme. Cys residues and position of disulfide bonds are highly conserved between the two structures of endoglucanases of A. germari. Surface calculation of agEGase structure in the absence of Cys residues reveals greater accessibility of the catalytic site to the substrate involving Asp42, a highly conserved residue. For the inhibition study, tannin-based structure was docked into the catalytic site of agEGase using ArgusLab 4.0 and it resulted in a stable complex formation. It is suggested that the inhibition could occur through formation of a stable transition state analog-enzyme complex with the tannin-based inhibitor, as observed with other insect cellulases in our laboratory.

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