Information on EC 3.5.1.105 - chitin disaccharide deacetylase

Word Map on EC 3.5.1.105
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.5.1.105
-
RECOMMENDED NAME
GeneOntology No.
chitin disaccharide deacetylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N,N'-diacetylchitobiose + H2O = N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
chitobiose degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-D-glucopyranose acetylhydrolase
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-beta-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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene chbG or ydjC; gene chbG or ydjC, encoded in the chb operon
UniProt
Manually annotated by BRENDA team
gene chbG or ydjC; gene chbG or ydjC, encoded in the chb operon
UniProt
Manually annotated by BRENDA team
no activity in Vibrio furnissii
no activity in Vibrio furnissii RIMD2223001
-
-
-
Manually annotated by BRENDA team
no activity in Vibrio nereis
no activity in Vibrio nereis NBRC15637
-
-
-
Manually annotated by BRENDA team
no activity in Vibrio orientalis
strain NBRC15638
-
-
Manually annotated by BRENDA team
strain NBRC15631
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain NBRC13287
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
show the reaction diagram
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
show the reaction diagram
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN + acetate
show the reaction diagram
GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcN + acetate
show the reaction diagram
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
?
show the reaction diagram
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
show the reaction diagram
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
show the reaction diagram
specific deacetylation at the nonreducing GlcNAc residue
-
-
?
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
show the reaction diagram
specific deacetylation at the nonreducing GlcNAc residue
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose + H2O
2-acetamido-4-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-2-deoxy-D-glucose + acetate
show the reaction diagram
GlcNAc-beta-(1,4)-GlcNAc + H2O
GlcNAc-beta-(1,4)-GlcN + acetate
show the reaction diagram
GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcN + acetate
show the reaction diagram
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc + H2O
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcN + acetate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
one Zn2+ ion is bound in the active site pocket. The zinc ion is coordinated by the triad consisting of an aspartic acid residue (Asp36) and two histidine residues (His93 and His97), which are located near the zinc ion
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
1 mM AgNO3, complete inhibition
Al3+
1 mM AlCl3, 30% inhibition
Cu2+
1 mM CuCl2, 53% inhibition
Fe2+
1 mM FeSO4, 26% inhibition
Hg2+
1 mM HgCl2, complete inhibition
Sn2+
1 mM SnCl2, 44% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31.8
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose
pH 8.5, 75°C
0.24 - 1.93
GlcNAc-beta-(1,4)-GlcNAc
98
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
pH 8.5, 75°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.6 - 29.5
GlcNAc-beta-(1,4)-GlcNAc
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.77
2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranose
Thermococcus kodakarensis
Q6F4N1
pH 8.5, 75°C
39638
11.2 - 122
GlcNAc-beta-(1,4)-GlcNAc
152260
0.0068
GlcNAc-beta-1,4-GlcNAc-beta-1,4-GlcNAc
Thermococcus kodakarensis
Q6F4N1
pH 8.5, 75°C
5421
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 11
pH 6.5: about 45% of maximal activity, pH 11: about 55% of maximal activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
about 50% of maximal activity at 30°C and 50°C
37 - 100
activity levels at 37°C and 100°C are about 20% of that observed at the optimal temperature (75°C)
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.3
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
6 * 30000, SDS-PAGE
31595
-
6 * 31595, calculated from sequence
31600
-
x * 31600, SDS-PAGE
44700
x * 44700, calculated from sequence
45000
-
x * 45000, SDS-PAGE
46000
-
x * 46000, SDS-PAGE
48000
x * 48000, SDS-PAGE
160000
gel filtration
174000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homohexamer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure is determined at resolutions of 1.54 A
-
the native enzyme and its selenomethionine derivative are crystallized and analyzed in the presence and absence of cadmium ion
-
crystal structure is determined at resolutions of 2.0 A
-
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 20 mg/ml protein in 20 mM sodium phosphate, pH 7.0, with an equal volume of reservoir solution containing 0.1 M Tris-HCl, pH 7.0, 10% w/v PEG 8000, and 0.2 M MgCl2, 4 weeks, 20°C, X-ray diffraction structure determination and analysis at 1.35 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
37°C, 20 min, about 75% loss of activity
696801
5
37°C, 20 min, about 40% loss of activity
696801
6 - 10
-
37°C, 60 min, stable
684604
7 - 11
37°C, 20 min, stable
696801
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
pH 7.5, 30 min, about 10% loss of activity
40
-
pH 7.0, 30 min, stable
50
pH 7.5, 30 min, about 40% loss of activity
70
pH 7.5, 30 min, about 80% loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, anion exchange chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of the soluble recombinant protein in Escherichia coli
gene chbG or ydjC, encoded in the chb operon, DNA and amino acid sequence determination and analysis
overexpressed as inclusion bodies in Escherichia coli Rosetta (DE3) pLys. The insoluble inclusion body is solubilized and reactivated through a refolding procedure
-
production of a recombinant chitin oligosaccharide deacetylase from Vibrio parahaemolyticus in the culture medium of Escherichia coli cells. The concentration of the recombinant enzyme in the Escherichia coli culture medium is 150times higher than that of wild-type enzyme produced in the culture medium by Vibrio parahaemolyticus KN1699
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added
the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added; the COD activity in the culture fluid to which GlcNAc-GlcN is added is higher than that to which (GlcNAc)2 is added
the transcription is specifically induced by GlcNAc2, suggesting the function of this gene in chitin catabolism in vivo. GlcNAc can not act as an inducer
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F146L
site-directed mutagenesis
K184E
site-directed mutagenesis
N137K/K184E
site-directed mutagenesis
N238S
site-directed mutagenesis
S134P
site-directed mutagenesis
F146L
-
site-directed mutagenesis
-
K184E
-
site-directed mutagenesis
-
N238S
-
site-directed mutagenesis
-
S134P
-
site-directed mutagenesis
-
additional information
Show AA Sequence (680 entries)
Please use the Sequence Search for a specific query.