Carbohydrate-active enzyme

CAZy, Carbohydrate-active enzymes, (2006) online database http //www.cazy. org 21.10.2006. 

P. M. Coutinho and B. Henrissat, 1999, Carbohydrate-Active Enzymes server at URL http //afmb.cnrs-mrs.fr/CAZY/. 

In the absence of structural data for many interesting glycosidases, comparison of their sequences has revealed important structural relationships and similarities of catalytic properties. The database CAZy (Carbohydrate-Active EnZymes) is a sequence-based collection of currently around 100 GH families (currently GH 1 to GH 117, with around 15 families deleted), which are further grouped in 14 clans. It provides family-typical structural and mechanistic details and has become an invaluable tool in GH research.98... 

As biochemical tools, suitable and sensible imino sugar modifications will certainly become helpful intelligent probes and reporters addressing some of the future needs of research in carbohydrate-active enzymes. 

In this section, enzymes in the EC 2.4. class are presented that catalyze valuable and interesting reactions in the field of polymer chemistry. The Enzyme Commission (EC) classification scheme organizes enzymes according to their biochemical function in living systems. Enzymes can, however, also catalyze the reverse reaction, which is very often used in biocatalytic synthesis. Therefore, newer classification systems were developed based on the three-dimensional structure and function of the enzyme, the property of the enzyme, the biotransformation the enzyme catalyzes etc. [88-93]. The Carbohydrate-Active enZYmes Database (CAZy), which is currently the best database/classification system for carbohydrate-active enzymes uses an amino-acid-sequence-based classification and would classify some of the enzymes presented in the following as hydrolases rather than transferases (e.g. branching enzyme, sucrases, and amylomaltase) [91]. Nevertheless, we present these enzymes here because they are transferases according to the EC classification. 

P. M. Coutinho, B. Henrissat, in Recent Advances in Carbohydrate Bioengineering (Eds. H.). H.). Gilbert, G. Davies, B. Henrissat, B. Svensson), The Royal Society of Chemistry, Cambridge, 1999, p. 3 P. M. Coutinho, B. Henrissat, Carbohydrate Active Enzymes database http //afmb.cnrs-mrs.ff/CAZY/ 1999. 

Gideon J. Davies (United Kingdom) Carbohydrate-active enzymes how Nature makes and breaks glycosides... 

B. Henrissat A journey through families of carbohydrate-active enzymes Y. Ito Synthesis and functional analysis of glycoprotein glycan chains... 

CAZy Carbohydrate active enzymes EMP Summary of enzy literatures... 

Coutinho, P., and Henrissat, B. 1999. The modular structure of cellulases and other carbohydrate-active enzymes an integrated database approach. In Ohmiya, K., Hayashi, K., Sakka, K., Kobayashi, Y., Karita, S., and Kimura, T. (Eds.), Genetics, Biochemistry and Ecology of Cellulose Degradation. Tokyo Uni Publishers Co., Ltd. 

Taniguchi, H. 2005. Carbohydrate active-enzymes for the production of oligosaccharides. In Hou, Ching T. (Ed.), Flandbook of Industrial Biocatalysis (ch 20). London Taylor Francis. 

Coutinho, P.M. and Henrissat, B. (1999) Carbohydrate-active enzymes an integrated database approach, in Recent Advances in Carbohydrate Bioengineering... 

Henrissat B, Coutinho PM, Davies GJ. A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana. Plant Molec. Biol. 2001 47 55-72. 

But of course the physical chemists standby of sucrose should not be used, because at the concentrations required ( M) it will bind to any carbohydrate-active enzyme. 

As is evident from the work that is reviewed here, the application of biocatalysts in preparative carbohydrate synthesis has continued to expand and diversify in recent years. Of particular note is the reengineering of biocatalyst properties (e.g., substrate specificity, stability) by the process of directed evolution. Significant progress in the study of the enzymatic biosynthesis of complex carbohydrate has been made with the development in protein purification, molecular genetics, and new methods of enzymological analysis. Bioinformatics provides a large number of putative candidates for carbohydrate-active enzymes. The combined... 

Davies GJ, Gloster TM, Henrissat B. Recent structural insights into the expanding world of carbohydrate-active enzymes. Curr Opinion Struct Biol 2005 15 637-645. 

Davies GJ, Henrissat B. Structural enzymology of carbohydrate-active enzymes implications for the post-genomic era. Biochem Soc Trans 2002 30 291-297. 

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