BRENDA - Enzyme Database show
show all sequences of 3.1.1.41

A novel cephalosporin deacetylating acetyl xylan esterase from Bacillus subtilis with high activity toward cephalosporin C and 7-aminocephalosporanic acid

Tian, Q.; Song, P.; Jiang, L.; Li, S.; Huang, H.; Appl. Microbiol. Biotechnol. 98, 2081-2089 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene Cah, subcloning in Escherichia coli strain JM109, expression in Escherichia coli strain BL21(DE3), the enzyme is secreted
Bacillus subtilis
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ag+
-
Bacillus subtilis
Ba2+
low inhibition at 1 mM
Bacillus subtilis
Ca2+
low inhibition at 1 mM
Bacillus subtilis
Cd2+
low inhibition at 1 mM
Bacillus subtilis
Co2+
low inhibition at 1 mM
Bacillus subtilis
Cu2+
strong inhibition at 1 mM
Bacillus subtilis
diethyldicarbonate
-
Bacillus subtilis
Fe2+
low inhibition at 1 mM
Bacillus subtilis
Fe3+
strong inhibition at 1 mM
Bacillus subtilis
Mg2+
low inhibition at 1 mM
Bacillus subtilis
Mn2+
low inhibition at 1 mM
Bacillus subtilis
additional information
no inhibition by EDTA and K+
Bacillus subtilis
PMSF
-
Bacillus subtilis
SDS
low inhibition at 1 mM
Bacillus subtilis
Zn2+
strong inhibition at 1 mM
Bacillus subtilis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
6 * 36000, recombinant enzyme, SDS-PAGE
Bacillus subtilis
223000
-
recombinant enzyme, gel filtration
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Bacillus subtilis
the enzyme has a double specificity on both the acetylated oligosaccharide, cf. EC 3.1.1.72, and cephalosporin C and 7-aminocephalosporanic acid
?
-
-
-
additional information
Bacillus subtilis CICC 20034
the enzyme has a double specificity on both the acetylated oligosaccharide, cf. EC 3.1.1.72, and cephalosporin C and 7-aminocephalosporanic acid
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
M1JUH6
gene Cah
-
Bacillus subtilis CICC 20034
M1JUH6
gene Cah
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme 1.2fold from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, gel filtration, dialysis, and ultrafiltration
Bacillus subtilis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.72
-
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-nitrophenyl butyrate
Bacillus subtilis
741
-
purified recombinant enzyme, pH 7.0, 40°C, substrate alpha-naphthyl acetate
Bacillus subtilis
962
-
purified recombinant enzyme, pH 7.0, 40°C, substrate beta-naphthyl acetate
Bacillus subtilis
1086
-
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-methylumbelliferyl acetate
Bacillus subtilis
1245
-
purified recombinant enzyme, pH 7.0, 40°C, substrate glucose pentacetate
Bacillus subtilis
2949
-
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-nitrophenyl acetate
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-naphthyl acetate + H2O
-
729073
Bacillus subtilis
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
-
729073
Bacillus subtilis CICC 20034
2-naphthol + acetate
-
-
-
?
3-naphthyl acetate + H2O
-
729073
Bacillus subtilis
3-naphthol + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
-
729073
Bacillus subtilis
4-methylumbelliferol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
-
729073
Bacillus subtilis
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
-
729073
Bacillus subtilis CICC 20034
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl butyrate + H2O
-
729073
Bacillus subtilis
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
-
729073
Bacillus subtilis CICC 20034
4-nitrophenol + butyrate
-
-
-
?
glucose pentacetate + H2O
-
729073
Bacillus subtilis
?
-
-
-
?
additional information
the enzyme has a double specificity on both the acetylated oligosaccharide, cf. EC 3.1.1.72, and cephalosporin C and 7-aminocephalosporanic acid
729073
Bacillus subtilis
?
-
-
-
-
additional information
the enzyme hydrolyzes the ester linkages of the acetyl groups in both the xylose moieties of the acetylated xylan fragments
729073
Bacillus subtilis
?
-
-
-
-
additional information
the enzyme has a double specificity on both the acetylated oligosaccharide, cf. EC 3.1.1.72, and cephalosporin C and 7-aminocephalosporanic acid
729073
Bacillus subtilis CICC 20034
?
-
-
-
-
additional information
the enzyme hydrolyzes the ester linkages of the acetyl groups in both the xylose moieties of the acetylated xylan fragments
729073
Bacillus subtilis CICC 20034
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
hexamer
6 * 36000, recombinant enzyme, SDS-PAGE
Bacillus subtilis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
-
assay at
Bacillus subtilis
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
30
75
activity range, profile overview
Bacillus subtilis
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
purified recombinant enzyme, pH 7.0, stable up to, loss of 10% activity after 120 h
Bacillus subtilis
50
-
purified recombinant enzyme, pH 7.0, loss of 20% activity after 120 h; purified recombinant enzyme, pH 7.0, loss of 60% activity after 120 h
Bacillus subtilis
60
-
purified recombinant enzyme, pH 7.0, inactivation within 10 h
Bacillus subtilis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Bacillus subtilis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
10
activity range, profile overview
Bacillus subtilis
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
4.5
12
purified recombinant enzyme, over 80% of maximal activity within this range
Bacillus subtilis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene Cah, subcloning in Escherichia coli strain JM109, expression in Escherichia coli strain BL21(DE3), the enzyme is secreted
Bacillus subtilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ag+
-
Bacillus subtilis
Ba2+
low inhibition at 1 mM
Bacillus subtilis
Ca2+
low inhibition at 1 mM
Bacillus subtilis
Cd2+
low inhibition at 1 mM
Bacillus subtilis
Co2+
low inhibition at 1 mM
Bacillus subtilis
Cu2+
strong inhibition at 1 mM
Bacillus subtilis
diethyldicarbonate
-
Bacillus subtilis
Fe2+
low inhibition at 1 mM
Bacillus subtilis
Fe3+
strong inhibition at 1 mM
Bacillus subtilis
Mg2+
low inhibition at 1 mM
Bacillus subtilis
Mn2+
low inhibition at 1 mM
Bacillus subtilis
additional information
no inhibition by EDTA and K+
Bacillus subtilis
PMSF
-
Bacillus subtilis
SDS
low inhibition at 1 mM
Bacillus subtilis
Zn2+
strong inhibition at 1 mM
Bacillus subtilis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
6 * 36000, recombinant enzyme, SDS-PAGE
Bacillus subtilis
223000
-
recombinant enzyme, gel filtration
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Bacillus subtilis
the enzyme has a double specificity on both the acetylated oligosaccharide, cf. EC 3.1.1.72, and cephalosporin C and 7-aminocephalosporanic acid
?
-
-
-
additional information
Bacillus subtilis CICC 20034
the enzyme has a double specificity on both the acetylated oligosaccharide, cf. EC 3.1.1.72, and cephalosporin C and 7-aminocephalosporanic acid
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme 1.2fold from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, gel filtration, dialysis, and ultrafiltration
Bacillus subtilis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.72
-
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-nitrophenyl butyrate
Bacillus subtilis
741
-
purified recombinant enzyme, pH 7.0, 40°C, substrate alpha-naphthyl acetate
Bacillus subtilis
962
-
purified recombinant enzyme, pH 7.0, 40°C, substrate beta-naphthyl acetate
Bacillus subtilis
1086
-
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-methylumbelliferyl acetate
Bacillus subtilis
1245
-
purified recombinant enzyme, pH 7.0, 40°C, substrate glucose pentacetate
Bacillus subtilis
2949
-
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-nitrophenyl acetate
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-naphthyl acetate + H2O
-
729073
Bacillus subtilis
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
-
729073
Bacillus subtilis CICC 20034
2-naphthol + acetate
-
-
-
?
3-naphthyl acetate + H2O
-
729073
Bacillus subtilis
3-naphthol + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
-
729073
Bacillus subtilis
4-methylumbelliferol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
-
729073
Bacillus subtilis
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
-
729073
Bacillus subtilis CICC 20034
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl butyrate + H2O
-
729073
Bacillus subtilis
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
-
729073
Bacillus subtilis CICC 20034
4-nitrophenol + butyrate
-
-
-
?
glucose pentacetate + H2O
-
729073
Bacillus subtilis
?
-
-
-
?
additional information
the enzyme has a double specificity on both the acetylated oligosaccharide, cf. EC 3.1.1.72, and cephalosporin C and 7-aminocephalosporanic acid
729073
Bacillus subtilis
?
-
-
-
-
additional information
the enzyme hydrolyzes the ester linkages of the acetyl groups in both the xylose moieties of the acetylated xylan fragments
729073
Bacillus subtilis
?
-
-
-
-
additional information
the enzyme has a double specificity on both the acetylated oligosaccharide, cf. EC 3.1.1.72, and cephalosporin C and 7-aminocephalosporanic acid
729073
Bacillus subtilis CICC 20034
?
-
-
-
-
additional information
the enzyme hydrolyzes the ester linkages of the acetyl groups in both the xylose moieties of the acetylated xylan fragments
729073
Bacillus subtilis CICC 20034
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
hexamer
6 * 36000, recombinant enzyme, SDS-PAGE
Bacillus subtilis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
-
assay at
Bacillus subtilis
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
30
75
activity range, profile overview
Bacillus subtilis
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
purified recombinant enzyme, pH 7.0, stable up to, loss of 10% activity after 120 h
Bacillus subtilis
50
-
purified recombinant enzyme, pH 7.0, loss of 20% activity after 120 h; purified recombinant enzyme, pH 7.0, loss of 60% activity after 120 h
Bacillus subtilis
60
-
purified recombinant enzyme, pH 7.0, inactivation within 10 h
Bacillus subtilis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Bacillus subtilis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
10
activity range, profile overview
Bacillus subtilis
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
4.5
12
purified recombinant enzyme, over 80% of maximal activity within this range
Bacillus subtilis
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to carbohydrate esterase family 7
Bacillus subtilis
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to carbohydrate esterase family 7
Bacillus subtilis
Other publictions for EC 3.1.1.41
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
749261
Singh
Structural role of a conserve ...
Thermotoga maritima, Thermotoga maritima ATCC 43589, Thermotoga maritima DSM 3109
Proteins
85
694-708
2017
-
-
1
1
2
-
-
18
-
-
2
-
-
6
-
-
1
-
-
-
13
-
23
-
3
-
1
20
1
1
-
-
-
-
-
-
-
1
-
1
2
-
-
-
-
18
-
-
2
-
-
-
-
1
-
-
13
-
23
-
3
-
1
20
1
1
-
-
-
-
-
-
19
19
746975
Singh
Crystal structure of Thermoto ...
Thermotoga maritima, Thermotoga maritima ATCC 43589, Thermotoga maritima DSM 3109
Biochem. Biophys. Res. Commun.
476
63-68
2016
-
-
-
1
-
-
-
-
-
-
-
-
-
8
-
-
1
-
-
-
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
749834
Ma
-
High-level expression of Ceph ...
Bacillus subtilis, Bacillus subtilis SIL3
Biochem. Eng. J.
114
183-190
2016
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
749837
Ma
-
One-pot enzymatic production ...
Pseudomonas sp. SE83
Biochem. Eng. J.
95
1-8
2015
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
752071
Tao
-
Efficient production of perac ...
Bacillus subtilis
Process Biochem.
50
2121-2127
2015
-
-
1
-
1
-
1
5
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
5
-
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
5
5
729073
Tian
A novel cephalosporin deacetyl ...
Bacillus subtilis, Bacillus subtilis CICC 20034
Appl. Microbiol. Biotechnol.
98
2081-2089
2014
-
-
1
-
-
-
15
-
-
-
2
2
-
2
-
-
1
-
-
-
6
-
13
1
1
1
3
-
1
1
1
-
-
-
-
-
-
1
-
-
-
-
-
15
-
-
-
-
2
2
-
-
-
1
-
-
6
-
13
1
1
1
3
-
1
1
1
-
-
1
1
-
-
-
730072
Wang
Double knockout of beta-lactam ...
Escherichia coli, Escherichia coli JM105
J. Biosci. Bioeng.
113
737-741
2012
-
-
-
-
1
-
-
-
-
-
-
2
-
7
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
730907
Levisson
Functional and structural char ...
Thermotoga maritima
Proteins
80
1545-1559
2012
-
-
1
1
-
-
2
-
1
2
-
2
-
1
-
-
1
1
-
-
-
-
4
1
1
-
-
-
1
-
-
-
1
-
-
-
-
1
-
1
-
-
-
2
1
-
1
2
-
2
-
-
-
1
-
-
-
-
4
1
1
-
-
-
1
-
-
-
-
2
2
-
-
-
747164
Hedge
The structural basis for the ...
Thermotoga maritima, Thermotoga maritima DSM 3109
Biochim. Biophys. Acta
1824
1024-1030
2012
-
-
1
-
1
-
-
10
-
-
-
-
-
4
-
-
1
-
-
-
-
-
15
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
10
-
-
-
-
-
-
-
1
-
-
-
-
15
-
1
-
-
-
1
-
-
-
-
-
-
-
10
10
677538
Martinez-Martinez
A colorimetric assay for the d ...
Bacillus pumilus, Bacillus pumilus CECT 5072
Anal. Biochem.
369
210-217
2007
-
1
1
-
-
-
-
2
-
-
-
-
-
4
-
-
1
-
-
-
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
671502
Takimoto
Batch production of deacetyl 7 ...
Bacillus subtilis, Bacillus subtilis SHS0133
Appl. Microbiol. Biotechnol.
65
263-267
2004
-
1
1
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Abbott
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Hinnem
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Abraham
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Fujisawa
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