The Enzyme Database

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EC 2.4.1.280     
Accepted name: N,N′-diacetylchitobiose phosphorylase
Reaction: N,N′-diacetylchitobiose + phosphate = N-acetyl-D-glucosamine + N-acetyl-α-D-glucosamine 1-phosphate
Glossary: N,N′-diacetylchitobiose = N-acetyl-D-glucosaminyl-β-(1→4)-N-acetyl-D-glucosamine
Other name(s): chbP (gene name)
Systematic name: N,N′-diacetylchitobiose:phosphate N-acetyl-D-glucosaminyltransferase
Comments: The enzyme is specific for N,N′-diacetylchitobiose and does not phosphorylate other N-acetylchitooligosaccharides, cellobiose, trehalose, lactose, maltose or sucrose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Park, J.K., Keyhani, N.O. and Roseman, S. Chitin catabolism in the marine bacterium Vibrio furnissii. Identification, molecular cloning, and characterization of a N,N′-diacetylchitobiose phosphorylase. J. Biol. Chem. 275 (2000) 33077–33083. [DOI] [PMID: 10913116]
2.  Honda, Y., Kitaoka, M. and Hayashi, K. Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus: identification of family 36 glycosyltransferase in Vibrio. Biochem. J. 377 (2004) 225–232. [DOI] [PMID: 13678418]
3.  Hidaka, M., Honda, Y., Kitaoka, M., Nirasawa, S., Hayashi, K., Wakagi, T., Shoun, H. and Fushinobu, S. Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (α/α)6 barrel fold. Structure 12 (2004) 937–947. [DOI] [PMID: 15274915]
[EC 2.4.1.280 created 2012]
 
 
EC 2.7.1.196     
Accepted name: protein-Nπ-phosphohistidine—N,N′-diacetylchitobiose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + N,N′-diacetylchitobiose[side 1] = [protein]-L-histidine + N,N′-diacetylchitobiose 6′-phosphate[side 2]
Other name(s): chbABC (gene names); N,N′-diacetylchitobiose PTS permease; chitobiose PTS permease; EIIcel; EIIchb; Enzyme IIcel; Enzyme IIchb
Systematic name: protein-Nπ-phospho-L-histidine:N,N′-diacetylchitobiose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Keyhani, N.O., Wang, L.X., Lee, Y.C. and Roseman, S. The chitin disaccharide, N,N′-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system. J. Biol. Chem. 275 (2000) 33084–33090. [DOI] [PMID: 10913117]
2.  Reizer, J., Reizer, A. and Saier, M.H., Jr. The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus. Res. Microbiol. 141 (1990) 1061–1067. [DOI] [PMID: 2092358]
3.  Keyhani, N.O., Boudker, O. and Roseman, S. Isolation and characterization of IIAChb, a soluble protein of the enzyme II complex required for the transport/phosphorylation of N, N′-diacetylchitobiose in Escherichia coli. J. Biol. Chem. 275 (2000) 33091–33101. [DOI] [PMID: 10913118]
4.  Keyhani, N.O., Bacia, K. and Roseman, S. The transport/phosphorylation of N,N′-diacetylchitobiose in Escherichia coli. Characterization of phospho-IIB(Chb) and of a potential transition state analogue in the phosphotransfer reaction between the proteins IIA(Chb) AND IIB(Chb). J. Biol. Chem. 275 (2000) 33102–33109. [DOI] [PMID: 10913119]
[EC 2.7.1.196 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.196]
 
 
EC 3.2.1.200     
Accepted name: exo-chitinase (non-reducing end)
Reaction: Hydrolysis of N,N′-diacetylchitobiose from the non-reducing end of chitin and chitodextrins.
Other name(s): chiB (gene name)
Systematic name: (1→4)-2-acetamido-2-deoxy-β-D-glucan diacetylchitobiohydrolase (non-reducing end)
Comments: The enzyme hydrolyses the second glycosidic (1→4) linkage from non-reducing ends of chitin and chitodextrin molecules, liberating N,N′-diacetylchitobiose disaccharides. cf. EC 3.2.1.201, exo-chitinase (reducing end).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Tanaka, T., Fukui, T. and Imanaka, T. Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Biol. Chem. 276 (2001) 35629–35635. [DOI] [PMID: 11468293]
2.  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. [DOI] [PMID: 15717865]
3.  Ohnuma, T., Numata, T., Osawa, T., Mizuhara, M., Lampela, O., Juffer, A.H., Skriver, K. and Fukamizo, T. A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis. Planta 234 (2011) 123–137. [DOI] [PMID: 21390509]
4.  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. [DOI] [PMID: 23824666]
[EC 3.2.1.200 created 2017]
 
 
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 8757722]
[EC 3.2.1.201 created 2017]
 
 
EC 3.2.1.202     
Accepted name: endo-chitodextinase
Reaction: Hydrolysis of chitodextrins, releasing N,N′-diacetylchitobiose and small amounts of N,N′,N′′-triacetylchitotriose.
Other name(s): endo I (gene name); chitodextrinase (ambiguous); endolytic chitodextrinase; periplasmic chitodextrinase
Systematic name: (1→4)-2-acetamido-2-deoxy-β-D-glucan diacetylchitobiohydrolase (endo-cleaving)
Comments: The enzyme, characterized from the bacterium Vibrio furnissii, is an endo-cleaving chitodextrinase that participates in the the chitin catabolic pathway found in members of the Vibrionaceae. Unlike EC 3.2.1.14, chitinase, it has no activity on chitin. The smallest substrate is a tetrasaccharide, and the final products are N,N′-diacetylchitobiose and small amounts of N,N′,N′′-triacetylchitotriose. cf. EC 3.2.1.200, exo-chitinase (non-reducing end), and EC 3.2.1.201, exo-chitinase (reducing end).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bassler, B.L., Yu, C., Lee, Y.C. and Roseman, S. Chitin utilization by marine bacteria. Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii. J. Biol. Chem. 266 (1991) 24276–24286. [PMID: 1761533]
2.  Keyhani, N.O. and Roseman, S. The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic chitodextrinase. J. Biol. Chem. 271 (1996) 33414–33424. [DOI] [PMID: 8969204]
[EC 3.2.1.202 created 2017]
 
 
EC 3.5.1.105     
Accepted name: chitin disaccharide deacetylase
Reaction: N,N′-diacetylchitobiose + H2O = N-acetyl-β-D-glucosaminyl-(1→4)-D-glucosamine + acetate
Glossary: N,N′-diacetylchitobiose = N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine
Other name(s): chitobiose amidohydolase; COD; chitin oligosaccharide deacetylase; chitin oligosaccharide amidohydolase; 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]-2-deoxy-D-glucopyranose acetylhydrolase
Systematic name: N,N′-diacetylchitobiose acetylhydrolase
Comments: Chitin oligosaccharide deacetylase is a key enzyme in the chitin catabolic cascade of chitinolytic Vibrio strains. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio parahemolyticus [2]. In contrast to EC 3.5.1.41 (chitin deacetylase) this enzyme is specific for the chitin disaccharide [1,3]. It also deacetylates the chitin trisaccharide with lower efficiency [3]. No activity with higher polymers of GlcNAc [1,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kadokura, K., Rokutani, A., Yamamoto, M., Ikegami, T., Sugita, H., Itoi, S., Hakamata, W., Oku, T. and Nishio, T. Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin. Appl. Microbiol. Biotechnol. 75 (2007) 357–365. [DOI] [PMID: 17334758]
2.  Hirano, T., Kadokura, K., Ikegami, T., Shigeta, Y., Kumaki, Y., Hakamata, W., Oku, T. and Nishio, T. Heterodisaccharide 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a specific inducer of chitinolytic enzyme production in Vibrios harboring chitin oligosaccharide deacetylase genes. Glycobiology 19 (2009) 1046–1053. [DOI] [PMID: 19553519]
3.  Ohishi, K., Yamagishi, M., Ohta, T., Motosugi, M., Izumida, H., Sano, H., Adachi, K., Miwa, T. Purification and properties of two deacetylases produced by Vibrio alginolyticus H-8. Biosci. Biotechnol. Biochem. 61 (1997) 1113–1117.
4.  Ohishi, K., Murase, K., Ohta, T. and Etoh, H. Cloning and sequencing of the deacetylase gene from Vibrio alginolyticus H-8. J. Biosci. Bioeng. 90 (2000) 561–563. [DOI] [PMID: 16232910]
[EC 3.5.1.105 created 2010]
 
 
EC 3.5.1.136     
Accepted name: N,N′-diacetylchitobiose non-reducing end deacetylase
Reaction: N,N′-diacetylchitobiose + H2O = β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine + acetate
Other name(s): diacetylchitobiose deacetylase (ambiguous); cda (gene name)
Systematic name: N,N′-diacetylchitobiose non-reducing end acetylhydrolase
Comments: The enzyme, characterized from the archaeons Thermococcus kodakarensis and Pyrococcus horikoshii, deacetylates the non-reducing residue of N,N′-diacetylchitobiose, the end product of the archaeal chitinase, to produce β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine. This is in contrast to EC 3.5.1.105, chitin disaccharide deacetylase, which deacetylates N,N′-diacetylchitobiose at the reducing residue to produce N-acetyl-β-D-glucosaminyl-(1→4)-D-glucosamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Tanaka, T., Fukui, T., Fujiwara, S., Atomi, H. and Imanaka, T. Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Biol. Chem. 279 (2004) 30021–30027. [DOI] [PMID: 15136574]
2.  Mine, S., Ikegami, T., Kawasaki, K., Nakamura, T. and Uegaki, K. Expression, refolding, and purification of active diacetylchitobiose deacetylase from Pyrococcus horikoshii. Protein Expr. Purif. 84 (2012) 265–269. [DOI] [PMID: 22713621]
3.  Nakamura, T., Yonezawa, Y., Tsuchiya, Y., Niiyama, M., Ida, K., Oshima, M., Morita, J. and Uegaki, K. Substrate recognition of N,N′-diacetylchitobiose deacetylase from Pyrococcus horikoshii. J. Struct. Biol. 195:S1047-8477( (2016). [DOI] [PMID: 27456364]
[EC 3.5.1.136 created 2020]
 
 


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