Any feedback?
Information on EC 3.2.1.14 - chitinase and Organism(s) Serratia marcescens and UniProt Accession P11797
for references in articles please use BRENDA:EC3.2.1.14Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.14 chitinaseIUBMB Comments
The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo-chitodextrinases can act. Activity is greatly stimulated in the presence of EC 1.14.99.53, lytic chitin monoxygenase, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase. cf. EC 3.2.1.202, endo-chitodextrinase.
Specify your search results
Word Map
- 3.2.1.14
-
biocontrol
-
colloidal
- trichoderma
-
chitin-binding
- fusarium
-
pathogenesis-related
- serratia
- n-acetylglucosamine
- marcescens
- chitosan
-
3-like
-
chi3l1
- solani
-
freezing
- gaucher
- glcnac
- beta-1,3-glucanase
-
phytopathogenic
- cellulase
- rhizoctonia
- oxysporum
- cinerea
- botrytis
- glucanase
- harzianum
- mycelial
- cuticle
-
defense-related
-
hysteresis
-
rhizosphere
- colletotrichum
- chitooligosaccharides
-
molt
- n-acetyl-d-glucosamine
- alternaria
- flounder
- circulans
- chitosanase
-
entomopathogenic
-
recrystallization
- sclerotiorum
-
transglycosylation
- viride
- beauveria
- bassiana
- pythium
- nucleopolyhedrovirus
-
anthracnose
- glucocerebrosidase
- gloeosporioides
- environmental protection
- molecular biology
- analysis
- synthesis
- pharmacology
- industry
- degradation
- medicine
- biotechnology
- agriculture
The taxonomic range for the selected organisms is: Serratia marcescens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
chitinase, chitotriosidase, endochitinase, antifreeze protein, chit1, amcase, chitinase a, exochitinase, acidic mammalian chitinase, class i chitinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-poly-N-acetylglucosaminidase
-
-
-
-
beta-1,4-poly-N-acetyl glucosamidinase
-
-
-
-
CF-AG
-
-
-
-
CF-antigen
-
-
-
-
CHI-26
-
-
-
-
ChiA
ChiB
CHIT 1A
-
-
-
-
CHIT 1B
-
-
-
-
chitodextrinase-N-
-
-
-
-
Complement-fixation antigen
-
-
-
-
endochitinase
MF1 antigen
-
-
-
-
poly-beta-glucosaminidase
-
-
-
-
UDA
-
-
-
-
additional information
endochitinase
-
-
-
-
additional information
ChiB belongs to the family 18 of glycohydrolases
additional information
BJL200-ChiC1 belongs to the family 18 chitinases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
reaction mechanism, Glu315 is the acid/base during hydrolysis, the side-chain of the preceding Asp313 helps to position the N-acetyl moiety of the glycosyl sugar undergoing hydrolysis correctly, mutation of the conserved Tryp167 in the chitin-binding cleft of chitinase A enhances transglycosylation, transglycosylation reaction scheme, overview
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
double displacement reaction mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase
The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo-chitodextrinases can act. Activity is greatly stimulated in the presence of EC 1.14.99.53, lytic chitin monoxygenase, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase. cf. EC 3.2.1.202, endo-chitodextrinase.
CAS REGISTRY NUMBER
COMMENTARY
9001-06-3
-
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
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + ?
the polymer disappears very slowly, while the initially produced oligomers almost exclusively had even-numbered chain lengths in the 212 range. ChiB is a processive chitinase
-
-
?
4-methylumbelliferyl GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
4-methylumbelliferone + GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
-
-
-
-
?
4-methylumbelliferyl GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
?
-
-
-
?
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O
?
BJL200-ChiA and BJL200-ChiB have an approximately 30fold higher kcat and 15fold lower Km than BJL200-ChiC1 for the oligomeric substrate
-
-
?
4-nitrophenyl beta-N,N',N'',N'''-tetraacetylchitotetraoside + H2O
4-nitrophenol + beta-N,N',N'',N'''-tetraacetylchitotetraose
-
-
-
?
4-nitrophenyl beta-N,N',N''-triacetylchitotrioside + H2O
4-nitrophenol + beta-N,N',N''-triacetylchitotriose
-
-
-
?
4-nitrophenyl beta-N,N'-diacetylchitobioside + H2O
4-nitrophenol + beta-N,N'-diacetylchitobiose
-
-
-
?
beta-chitin + H2O
?
substrate 3 micrometer beta-chitin
-
-
?
cell wall + H2O
chitin oligosaccharides
-
from yeast
N-acetetylglucosamine and diacetylchitobiose
?
chitin + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose + N-acetylglucosamine
-
isoform ChiA is the most effective enzyme toward insoluble chitin, isoform ChiC1 is the most effective enzyme toward soluble chitin, ChiA, ChiB and ChiC1 hydrolyze water-soluble chitin very efficiently but powdered chitin is a very poor substrate
(GlcNAc)2 is almost exclusively generated from ChiA, ChiB and ChiC1, ChiA produced as minor products GlcNAc and (GlcNAc)3, ChiB produced as minor product only (GlcNAc)3, ChiC1 produced as minor product only GlcNAc
-
?
CM-chitin-RBV + H2O
?
BJL200-ChiC1 is 10-15times faster than BJL200-ChiB and BJL200-ChiA in degrading the polymeric substrate CM-chitin-RBV
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose + N,N',N''-triacetylchitotriose
-
-
ChiA almost exclusively generates (GlcNAc)2 and (GlcNAc)4, ChiB and ChiC1 generated all three products
-
?
chitin + H2O
?
-
crystalline beta-chitin, molecular weight analysis of oligomer products, overview
-
-
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
-
-
-
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
from ground crab shell
with high ratio of chitinase to chitin N-acetylglucosamine only
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
[acetyl-3H]chitin
-
-
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
[acetyl-3H]chitin
with high ratio of chitinase to chitin N-acetylglucosamine only
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
[acetyl-3H]chitin
diacetylchitobiose only, some trisaccharides in early stages
?
chitosan + H2O
?
-
chitosan with different degrees of deacetylation
-
-
?
chitosan + H2O
?
-
soluble chitin-derivative chitosan, molecular weight analysis of oligomer products, overview
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + ?
ChiC shows rapid disappearance of the polymer and production of a continuum of odd- and even-numbered oligomers. ChiC is a nonprocessive endochitinase
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + ?
the polymer disappears very slowly, while the initially produced oligomers almost exclusively had even-numbered chain lengths in the 212 range. ChiA is a processive chitinase
-
-
?
additional information
?
-
wild-type ChiA and mutant ChiAW167A substrate specificity, product determinations, overview, the enzyme also performs transglycosylation with chito-oligosaccharides as acceptors, overview
-
-
?
additional information
?
-
-
wild-type ChiA and mutant ChiAW167A substrate specificity, product determinations, overview, the enzyme also performs transglycosylation with chito-oligosaccharides as acceptors, overview
-
-
?
additional information
?
-
-
isozyme ChiA Nima shows high antibacterial activity against Enterobacter cloacae, Escherichia coli, Staphylococcus aureus and Staphylococcus xylosus, overview
-
-
?
additional information
?
-
-
aromatic residues in the catalytic center of chitinase A affect processivity, enzyme activity, and biomass converting efficiency. Progressivity of isozymes is dependent on the substrate, the processive mechanism is essential for an efficient conversion of crystalline substrates but comes at a large cost in terms of intrinsic enzyme speed, overview
-
-
?
additional information
?
-
the enzyme is also active with chitooligosachharides from GlnNAc to GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAc, overview
-
-
?
additional information
?
-
-
the enzyme is also active with chitooligosachharides from GlnNAc to GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAc, overview
-
-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
isozyme ChiA Nima shows high antibacterial activity against Enterobacter cloacae, Escherichia coli, Staphylococcus aureus and Staphylococcus xylosus, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
argadin
thermodynamics and enzyme-bound crystal structure, detailed overview
argifin
thermodynamics and enzyme-bound crystal structure, detailed overview
(1E)-prop-1-en-1-yl 2-(acetylamino)-4-O-[(2R,5R,6R)-5-(acetylamino)-2-(hydroxymethyl)-1,3-oxazinan-6-yl]-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside
-
potent inhibition, IC50 is 0.0047 mM, chemo-enzymatic synthesis via allyl penta-N-acetyl-chitopentaose using recombinant NodC from Mesorhizobium loti expressed in Escherichia coli, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0042
4-methylumbelliferyl beta-N,N',N''-triacetylchitotrioside
pH 6.5, isozyme ChiA
0.0068
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside
pH 6.5, isozyme ChiB
0.0798
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside
pH 6.5, isozyme ChiC
additional information
additional information
kinetics of wild-type and alpha/beta domain deletion mutant, overview
-
additional information
additional information
-
kinetics of wild-type and alpha/beta domain deletion mutant, overview
-
additional information
additional information
pH dependence of ChiC kinetics, overview
-
additional information
additional information
-
pH dependence of ChiC kinetics, overview
-
additional information
additional information
Michaelis-Menten kinetics, 3.30 mg/ml with colloidal chitin, pH 6.0, 50°C, recombinant enzyme
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside
pH 6.5, isozyme ChiC
56.8
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside
pH 6.5, isozyme ChiB
67.4
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside
pH 6.5, isozyme ChiA
9.2
beta-chitin
presence of lytic polysaccharide monooxygenase Cbp21, pH 6.1, 37°C
11.1
beta-chitin
presence of lytic polysaccharide monooxygenase Cbp21, pH 8.0, 37°C
13.9
beta-chitin
presence of lytic polysaccharide monooxygenase Cbp21, pH 8.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0047
(1E)-prop-1-en-1-yl 2-(acetylamino)-4-O-[(2R,5R,6R)-5-(acetylamino)-2-(hydroxymethyl)-1,3-oxazinan-6-yl]-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranoside
Serratia marcescens
-
potent inhibition, IC50 is 0.0047 mM, chemo-enzymatic synthesis via allyl penta-N-acetyl-chitopentaose using recombinant NodC from Mesorhizobium loti expressed in Escherichia coli, overview
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.9
with substrate 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside, isozyme ChiC
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme contains a 25 amino acid signal peptide and is secreted
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
phylogenetic analysis reveals the possibility of horizontal gene transfer between bacteria, viruses, and insects. The Chit62 enzyme is clearly grouped with other bacterial chitinases, but with a clear distinction from previously reported Serratia marcescens
physiological function
physiological function
the active enzyme shows biocontrol features against fungal phytopathogens
physiological function
in presence of lytic polysaccharide monooxygenase Cbp21, the apparent kcat values of chitinases ChiA and ChiB increase 6-9fold, while there is no effect on chitinase ChiC
physiological function
presence of CBP21 increases solubilization of chitin substrates with high degrees of crystallinity when combined with each of the three chitinases ChiA, ChiB, or ChiC, but this synergy is reduced upon decline in crystallinity
physiological function
presence of CBP21 increases solubilization of chitin substrates with high degrees of crystallinity when combined with each of the three chitinases ChiA, ChiB, or ChiC, but this synergy is reduced upon decline in crystallinity. Isoform ChiA shows lowest effects
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
58000
62000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the catalytic domain has a TIM-barrel fold, structure modelling, overview
additional information
-
the catalytic domain has a TIM-barrel fold, structure modelling, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of ChiB bound to argadin or to argifin, molecular modelling, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F396A
-
site-directed mutagenesis of the +2 subsite residue of isozyme ChiA, the mutant shows only modest reductions in processivity, and shows reduced efficiency toward chitin and an up to 20fold higher activity toward chitosan
W167A
W167A/W275A
-
site-directed mutagenesis of the -3 and +1 subsites residues of isozyme ChiA, the mutant shows reduced efficiency toward chitin and an up to 20fold higher activity toward chitosan
W275A
-
site-directed mutagenesis of the +1 subsite residue of isozyme ChiA, the mutant shows only modest reductions in processivity, and shows reduced efficiency toward chitin and an up to 20fold higher activity toward chitosan
additional information
W167A
site-directed mutagenesis, mutation of the conserved tryptophan in the chitin-binding cleft of chitinase A enhances transglycosylation
W167A
-
site-directed mutagenesis of the -3 subsite residue of isozyme ChiA, the mutant shows almost abolished progressivity, reduced efficiency toward chitin and an up to 20fold higher activity toward chitosan
additional information
an alpha + beta insertion between the B7 beta-strand and A7 alpha-helix of the TIM-barrel, an FnIII domain at the N-terminus of the molecule and a hinge region that connects the latter to the catalytic domain. Structure modelling of the (alpha + beta)DELTAChiA mutant, overview
additional information
-
an alpha + beta insertion between the B7 beta-strand and A7 alpha-helix of the TIM-barrel, an FnIII domain at the N-terminus of the molecule and a hinge region that connects the latter to the catalytic domain. Structure modelling of the (alpha + beta)DELTAChiA mutant, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
purified enzyme, 50°C, 1 h, over 50% activity remaing within this range, completely stable at pH 6.0-8.0
729155
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
ChiC1: 40% of activity remained, ChiA and ChiB: 10% of activity remained
60
ChiA exhibits an endothermic irreversible transition at an apparent Tm of 60.7°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme 5fold from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and dialysis
recombinant isozyme ChiC from Escherichia coli strain BL21(DE3) periplasm in a one step procedure using hydrophobic interaction chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 (DE3)
expression in Escherichia coli
gene chiC, expression of ChiC in Escherichia coli strain BL21(DE3) periplasm
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cabib, E.; Sburlati, A.
Enzymatic determination of chitin
Methods Enzymol.
161
457-459
1988
Serratia marcescens
-
Cabib, E.
Assay for chitinase using tritiated chitin
Methods Enzymol.
161
424-426
1988
Serratia marcescens, Triticum aestivum
-
Cabib, E.
Chitinase from Serratia marcescens
Methods Enzymol.
161
460-462
1988
Serratia marcescens
-
Ohtakara, A.; Izume, M.; Mitsutomi, M.
Action of microbial chitinases on chitosan with different degrees of deacetylation
Agric. Biol. Chem.
52
3181-3182
1988
Aeromonas hydrophila, Streptomyces sp., Serratia marcescens, Streptomyces antibioticus, Streptomyces griseus
-
Jones, J.D.G.; Grady, K.L.; Suslow, T.V.; Bedbrook, J.R.
Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens
EMBO J.
5
467-473
1986
Serratia marcescens
Roberts, R.L.; Cabib, E.
Serratia marcescens chitinase: one-step purification and use for the determination of chitin
Anal. Biochem.
127
402-412
1982
Serratia marcescens
Watanabe, T.; Kanai, R.; Kawase, T.; Tanabe, T.; Mitsutomi, M.; Sakuda, S.; Miyashita, K.
Family 19 chitinases of Streptomyces species: characterization and distribution
Microbiology
145
3353-3363
1999
Niallia circulans, Streptomyces sp., Serratia marcescens, Streptomyces atrovirens, Streptomyces coelicolor, Streptomyces cyanocolor, Streptomyces eurythermus, Streptomyces griseus, Streptomyces ipomoeae, Streptomyces lividans, Streptomyces plicatus, Streptomyces prasinopilosus, Streptomyces scabiei, Niallia circulans WL12, Streptomyces griseus HUT6037
Suzuki, K.; Sugawara, N.; Suzuki, M.; Uchiyama, T.; Katouno, F.; Nikaidou, N.; Watanabe, T.
Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: enzymatic properties and synergism on chitin degradation
Biosci. Biotechnol. Biochem.
66
1075-1083
2002
Serratia marcescens, Serratia marcescens 2170
van Aalten, D.M.; Komander, D.; Synstad, B.; Gaseidnes, S.; Peter, M.G.; Eijsink, V.G.
Structural insights into the catalytic mechanism of a family 18 exo-chitinase
Proc. Natl. Acad. Sci. USA
98
8979-8984
2001
Serratia marcescens (P11797), Serratia marcescens
Huang, G.L.; Zahng, D.W.; Zhao, H.J.; Zhang, H.C.; Wang, P.G.
Chemo-enzymatic synthesis of 1,4-oxazepanyl sugar as potent inhibitor of chitinase
Bioorg. Med. Chem.
14
2446-2449
2006
Serratia marcescens
Aronson, N.N.Jr.; Halloran, B.A
Alexeyev, M.F.; Zhou, X.E.; Wang, Y.; Meehan, E.J.; Chen, L.: Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation
Biosci. Biotechnol. Biochem.
70
243-251
2006
Serratia marcescens (P07254), Serratia marcescens
Horn, S.J.; Sorbotten, A.; Synstad, B.; Sikorski, P.; Sorlie, M.; Varum, K.M.; Eijsink, V.G.
Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens
FEBS J.
273
491-503
2006
Serratia marcescens (P07254), Serratia marcescens (P11797), Serratia marcescens (Q068W1), Serratia marcescens
Zees, A.C.; Pyrpassopoulos, S.; Vorgias, C.E.
Insights into the role of the (alpha+beta) insertion in the TIM-barrel catalytic domain, regarding the stability and the enzymatic activity of chitinase A from Serratia marcescens
Biochim. Biophys. Acta
1794
23-31
2009
Serratia marcescens (P07254), Serratia marcescens
Gouda, H.; Yanai, Y.; Sugawara, A.; Sunazuka, T.; Omura, S.; Hirono, S.
Computational analysis of the binding affinities of the natural-product cyclopentapeptides argifin and argadin to chitinase B from Serratia marcescens
Bioorg. Med. Chem.
16
3565-3579
2008
Serratia marcescens (P11797), Serratia marcescens
Synstad, B.; Vaaje-Kolstad, G.; Cederkvist, F.H.; Saua, S.F.; Horn, S.J.; Eijsink, V.G.; Sorlie, M.
Expression and characterization of endochitinase C from Serratia marcescens BJL200 and its purification by a one-step general chitinase purification method
Biosci. Biotechnol. Biochem.
72
715-723
2008
Serratia marcescens (Q700B8), Serratia marcescens, Serratia marcescens BJL200 (Q700B8), Serratia marcescens BJL200
Barboza-Corona, J.E.; Gutierrez-Acosta, O.B.; Imperial-Cervantes, M.; Bideshi, D.K.; de la Fuente-Salcido, N.; Bautista-Justo, M.; Salcedo-Hernandez, R.
Generation of antibacterial oligosaccharides derived from chitin using heterologous endochitinase synthesized in Escherichia coli
J. Appl. Microbiol.
105
1511-1520
2008
Bacillus thuringiensis, Serratia marcescens
Zakariassen, H.; Aam, B.B.; Horn, S.J.; Varum, K.M.; Soerlie, M.; Eijsink, V.G.
Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency
J. Biol. Chem.
284
10610-10617
2009
Serratia marcescens, Serratia marcescens BJL200
Duzhak, A.B.; Panfilova, Z.I.; Duzhak, T.G.; Vasyunina, E.A.
Extracellular chitinases of mutant superproducing strain Serratia marcescens M-1
Biochemistry (Moscow)
74
209-214
2009
Serratia marcescens (P07254), Serratia marcescens (P11797), Serratia marcescens (Q8VQN1), Serratia marcescens
Babashpour, S.; Aminzadeh, S.; Farrokhi, N.; Karkhane, A.; Haghbeen, K.
Characterization of a chitinase (Chit62) from Serratia marcescens B4A and its efficacy as a bioshield against plant fungal pathogens
Biochem. Genet.
50
722-735
2012
Serratia marcescens (E5FGC5), Serratia marcescens B4A (E5FGC5), Serratia marcescens B4A
Hamre, A.G.; Eide, K.B.; Wold, H.H.; Sorlie, M.
Activation of enzymatic chitin degradation by a lytic polysaccharide monooxygenase
Carbohydr. Res.
407
166-169
2015
Serratia marcescens (P07254), Serratia marcescens (Q54276)
Nakagawa, Y.S.; Eijsink, V.G.; Totani, K.; Vaaje-Kolstad, G.
Conversion of alpha-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
11061-11066
2013
Serratia marcescens, Serratia marcescens (P07254), Serratia marcescens (Q54276)
EXTERNAL LINKS (specific for EC-Number 3.2.1.14)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
