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Enzyme Nomenclature
Information on EC 3.2.1.200 - exo-chitinase (non-reducing end) and Organism(s) Serratia marcescens and UniProt Accession P11797
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3.2.1.200 exo-chitinase (non-reducing end)IUBMB 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).
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The taxonomic range for the selected organisms is: Serratia marcescens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Hydrolysis of N,N'-diacetylchitobiose from the non-reducing end of chitin and chitodextrins
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ChiB
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
(1->4)-2-acetamido-2-deoxy-beta-D-glucan diacetylchitobiohydrolase (non-reducing end)
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).
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl beta-D-N,N'-diacetylchitobioside + H2O
4-methylumbelliferone + beta-D-N,N'-diacetylchitobiose
-
-
-
?
4-methylumbelliferyl beta-D-N,N'-diacetylchitobioside + H2O
?
-
-
-
?
beta-chitin + H2O
?
-
ChiB is active from the nonreducing end to the reducing end
-
?
crystalline beta-chitin + H2O
N,N'-diacetylchitobiose + ?
the enzyme degrades the chitin from the non-reducing end
-
-
?
chitosan + H2O
?
-
65% acetylated chitosan, enzyme shows a processive mode of action, moving the sugar chain two residues at a time and almost exclusively yielding oligomers with even-numbered chain lengths
-
?
colloidal chitin + H2O
N-acetylglucosamine + N,N'-diacetylchitobiose + ?
-
ChiB produces relatively large amounts of chitin monomer and dimer, but very low amounts of trimer
-
?
additional information
?
-
ChiB is an exoenzyme which degrades the polymer chains from their nonreducing ends. The degradation of chitosan with 65% acetylated units showed biphasic kinetics: the faster phase is dominated by cleavage on the reducing side of two acetylated units (occupying subsites -2 and -1), while the slower kinetic phase reflects cleavage on the reducing side of a deacetylated and an acetylated unit (bound to subsites -2 and -1, respectively). The enzyme does not show preferences with respect to acetylation of the sugar bound in the +1 subsite. Even chitosans with low degrees of acetylation can be degraded by ChiB
-
-
?
additional information
?
-
-
processive enzyme, in which the substrate remains bound to the active cleft after successful hydrolysis and is moved along for the next hydrolysis to occur. ChiB performs on average 3.4 cleavages, for the formation of each enzyme-substrate complex. The exo-type of activity observed for ChiB during the degradation of solid crystalline chitin is due to the better accessibility of chain ends. When hydrolyzing soluble substrates, ChiB operates in a processive endo-attack mode of action
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
digestion of beta-chitin by ChiB occurs from the nonreducing end to the reducing end. Chitinases ChiA and ChiB show synergistic interactions in simultaneous degradation of beta-chitin, but not of glycol chitin
physiological function
reactions containing both ChiB and endochitinase ChiC show significantly increased N-acetylglucosamine trimer and dimer formation, but decreased monomer formation, compared to reactions with either enzyme alone. ChiB and ChiC attack different sites and together degrade chitin more efficiently than either enzyme separately. Chitobiase and chitin binding protein in combination with ChiB and ChiC (individually or together) increase their chitinase activity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ChiB comprises a catalytic (beta/alpha)8 barrel domain and a C-terminal putative chitin-binding domain. The cocrystallized chito-oligosaccharide is inserted into the catalytic cleft from the non-reducing end when digested by ChiB
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D142A
the mutation leads to almost complete loss of enzyme activity
Y214A
the mutation leads to reduced activity compared to the wild type enzyme
Y214F
the mutation leads to reduced activity compared to the wild type enzyme
Y240W
the mutant retains its substrate-binding ability but shows significantly decreased hydrolytic activity against crystalline beta-chitin compared to the wild type enzyme
Y240W/Y481W
the mutant retains its substrate-binding ability but shows significantly decreased hydrolytic activity against crystalline beta-chitin compared to the wild type enzyme
Y481W
the mutant retains its substrate-binding ability and shows wild type hydrolytic activity against crystalline beta-chitin
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
when applied in combination, a mixture of purified chitinases ChiA, ChiB and ChiC shows a toxic effect similar to that of benzimidazole on ascospore germination of Mycosphaerella fijiensis, causal agent of black Sigatoka in banana
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hult, E.L.; Katouno, F.; Uchiyama, T.; Watanabe, T.; Sugiyama, J.
Molecular directionality in crystalline beta-chitin: hydrolysis by chitinases A and B from Serratia marcescens 2170
Biochem. J.
388
851-856
2005
Serratia marcescens (P11797), Serratia marcescens 2170 (P11797)
Sikorski, P.; Sorbotten, A.; Horn, S.J.; Eijsink, V.G.; Varum, K.M.
Serratia marcescens chitinases with tunnel-shaped substrate-binding grooves show endo activity and different degrees of processivity during enzymatic hydrolysis of chitosan
Biochemistry
45
9566-9574
2006
Serratia marcescens
Gutierrez-Roman, M.; Holguin-Melendez, F.; Dunn, M.; Guillen-Navarro, K.; Huerta-Palacios, G.
Antifungal activity of Serratia marcescens CFFSUR-B2 purified chitinolytic enzymes and prodigiosin against Mycosphaerella fijiensis, causal agent of black Sigatoka in banana (Musa spp.)
BioControl
60
565-572
2015
Serratia marcescens (R9WYJ0), Serratia marcescens CFFSUR-B2 (R9WYJ0)
-
Sorbotten, A.; Horn, S.J.; Eijsink, V.G.; Varum, K.M.
Degradation of chitosans with chitinase B from Serratia marcescens. Production of chito-oligosaccharides and insight into enzyme processivity
FEBS J.
272
538-549
2005
Serratia marcescens (Q54276)
Gutierrez-Roman, M.I.; Dunn, M.F.; Tinoco-Valencia, R.; Holguin-Melendez, F.; Huerta-Palacios, G.; 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
33-42
2014
Serratia marcescens (R9WYJ0), Serratia marcescens CFFSUR-B2 (R9WYJ0)
Hamre, A.G.; Froberg, E.E.; Eijsink, V.G.H.; Sorlie, M.
Thermodynamics of tunnel formation upon substrate binding in a processive glycoside hydrolase
Arch. Biochem. Biophys.
620
35-42
2017
Serratia marcescens (P11797)
Koseki, J.; Gouda, H.; Hirono, S.
Molecular orbital study of the formation of intramolecular hydrogen bonding of a ligand molecule in a protein aromatic hydrophobic pocket
Chem. Pharm. Bull.
64
1031-1035
2016
Serratia marcescens (P11797)
Sugimoto, H.; Nakamura, K.; Nishino, Y.; Idezawa, Y.; Fujinuma, A.; Suzuki, K.; Watanabe, T.
Differences in the roles of the two surface-exposed tyrosine residues, Y240 and Y481, of Serratia marcescens chitinase B during processive degradation of crystalline chitin
J. Gen. Appl. Microbiol.
61
255-261
2016
Serratia marcescens (P11797), Serratia marcescens 2170 (P11797)
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Release 2023.1 (January 2023)
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