The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 3.2.1.201     
Accepted name: exo-chitinase (reducing end)
Reaction: Hydrolysis of N,N′-diacetylchitobiose from the reducing end of chitin and chitodextrins.
Other name(s): chiA (gene name)
Systematic name: (1→4)-2-acetamido-2-deoxy-β-D-glucan diacetylchitobiohydrolase (reducing end)
Comments: The enzyme hydrolyses the second glycosidic (1→4) linkage from reducing ends of chitin and chitodextrin molecules, liberating N,N′-diacetylchitobiose disaccharides. cf. EC 3.2.1.200, exo-chitinase (non-reducing end).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hult, E.L., Katouno, F., Uchiyama, T., Watanabe, T. and Sugiyama, J. Molecular directionality in crystalline β-chitin: hydrolysis by chitinases A and B from Serratia marcescens 2170. Biochem. J. 388 (2005) 851–856. [PMID: 15717865]
2.  Nakagawa, Y.S., Eijsink, V.G., Totani, K. and Vaaje-Kolstad, G. Conversion of α-chitin substrates with varying particle size and crystallinity reveals substrate preferences of the chitinases and lytic polysaccharide monooxygenase of Serratia marcescens. J. Agric. Food Chem. 61 (2013) 11061–11066. [PMID: 24168426]
3.  Gutierrez-Roman, M.I., Dunn, M.F., Tinoco-Valencia, R., Holguin-Melendez, F., Huerta-Palacios, G. and Guillen-Navarro, K. Potentiation of the synergistic activities of chitinases ChiA, ChiB and ChiC from Serratia marcescens CFFSUR-B2 by chitobiase (Chb) and chitin binding protein (CBP). World J Microbiol Biotechnol 30 (2014) 33–42. [PMID: 23824666]
4.  Brurberg, M.B., Nes, I.F. and Eijsink, V.G. Comparative studies of chitinases A and B from Serratia marcescens. Microbiology 142 (1996) 1581–1589. [PMID: 8757722]
[EC 3.2.1.201 created 2017]
 
 


Data © 2001–2017 IUBMB
Web site © 2005–2017 Andrew McDonald