From bacteria to human: A journey into the world of chitinases

被引：179

作者：

Adrangi, Sina ^{[1
]}

Faramarzi, Mohammad Ali ^{[2
,3
]}

机构：

[1] Shahid Beheshti Univ Med Sci, Sch Pharm, Dept Pharmaceut Biotechnol, Tehran, Iran

[2] Univ Tehran Med Sci, Fac Pharm, Dept Pharmaceut Biotechnol, Tehran 14176, Iran

[3] Univ Tehran Med Sci, Biotechnol Res Ctr, Dept Pharmaceut Biotechnol, Tehran 14176, Iran

来源：

BIOTECHNOLOGY ADVANCES | 2013年 / 31卷 / 08期

关键词：

Chitinase; Chi-lectin; Gene evolution; Biocontrol; Biomarker; ACIDIC MAMMALIAN CHITINASE; CHITINOLYTIC ACTIVITY; BINDING PROTEIN; DIFFERENTIAL EXPRESSION; CELLULOSE BIOSYNTHESIS; FAMILY-18; CHITINASE; SERRATIA-MARCESCENS; FUNGAL CHITINASES; CATALYTIC DOMAIN; TISSUE RESPONSES;

D O I：

10.1016/j.biotechadv.2013.09.012

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Chitinases, the enzymes responsible for the biological degradation of chitin, are found in a wide range of organisms from bacteria to higher plants and animals. They participate in numerous physiological processes such as nutrition, parasitism, morphogenesis and immunity. Many organisms, in addition to chitinases, produce inactive chitinase-like lectins that despite lacking enzymatic activity are involved in several regulatory functions. Most known chitinases belong to families 18 and 19 of glycosyl hydrolases, however a few chitinases that belong to families 23 and 48 have also been identified in recent years. In this review, different aspects of chitinases and chi-lectins from bacteria, fungi, insects, plants and mammals are discussed. (C) 2013 Elsevier Inc. All rights reserved.

引用

页码：1786 / 1795

页数：10

共 181 条

[1] Production of Chitooligosaccharides and Their Potential Applications in Medicine [J].

Aam, Berit B. ;

Heggset, Ellinor B. ;

Norberg, Anne Line ;

Sorlie, Morten ;

Varum, Kjell M. ;

Eijsink, Vincent G. H. .

MARINE DRUGS, 2010, 8 (05) :1482-1517

[2] New lives for old: evolution of pseudoenzyme function illustrated by iRhoms [J].

Adrain, Colin ;

Freeman, Matthew .

NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2012, 13 (08) :489-498

[3] Purification and characterization of two extracellular endochitinases from Massilia timonae [J].

Adrangi, Sina ;

Faramarzi, Mohammad Ali ;

Shahverdi, Ahmad Reza ;

Sepehrizadeh, Zargham .

CARBOHYDRATE RESEARCH, 2010, 345 (03) :402-407

[4]

Agapov E, 2009, AM J RESP CELL MOL, V41, P379, DOI [10.1165/2009-0122R, 10.1165/2009-0122RC]

[5]

Ahmadi K., 2008, Research Journal of Microbiology, V3, P395, DOI [10.3923/jm.2008.395.404, DOI 10.3923/JM.2008.395.404]

[6]

AHMADI K.J., 2008, BIOTECHNOLOGY, V7, P266, DOI [DOI 10.3923/BI0TECH.2008.266.272, DOI 10.3923/BIOTECH.2008.266.272]

[7] Attenuation of Pseudomonas aeruginosa virulence factors and biofilms by co-encapsulation of bismuth-ethanedithiol with tobramycin in liposomes [J].

Alipour, Misagh ;

Suntres, Zacharias E. ;

Lafrenie, Robert M. ;

Omri, Abdelwahab .

JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY, 2010, 65 (04) :684-693

[8]

Amian Awah Anna, 2011, GM Crops, V2, P104, DOI 10.4161/gmcr.2.2.16125

[9] Genetic association between human chitinases and lung function in COPD [J].

Aminuddin, F. ;

Akhabir, L. ;

Stefanowicz, D. ;

Pare, P. D. ;

Connett, J. E. ;

Anthonisen, N. R. ;

Fahy, J. V. ;

Seibold, M. A. ;

Burchard, E. G. ;

Eng, C. ;

Gulsvik, A. ;

Bakke, P. ;

Cho, M. H. ;

Litonjua, A. ;

Lomas, D. A. ;

Anderson, W. H. ;

Beaty, T. H. ;

Crapo, J. D. ;

Silverman, E. K. ;

Sandford, A. J. .

HUMAN GENETICS, 2012, 131 (07) :1105-1114

[10] Natural product family 18 chitinase inhibitors [J].

Andersen, OA ;

Dixon, MJ ;

Eggleston, IM ;

van Aalten, DMF .

NATURAL PRODUCT REPORTS, 2005, 22 (05) :563-579

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