Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) bis(1-methylcyclopropane-1-carboxylate) + H2O
?
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) bis(2-methylacrylate) + H2O
?
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) dicyclobutanecarboxylate + H2O
?
1,2,3,4-tetra-O--acetyl-xylopyranose + H2O
?
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
2,3,2',3',4'-penta-acetyl-xylobiose + H2O
?
-
-
?
2-(2-oxo-1,3-dihydroindol-3-yl) acetic acid + H2O
?
2-naphthyl acetate + H2O
2-naphthol + acetate
3'-O-acetyl-2'-deoxyadenosine + H2O
?
-
-
?
3-naphthyl acetate + H2O
3-naphthol + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
4-nitrophenyl-beta-D-xylopyranoside monoacetates as substrates in a beta-xylosidase-coupled assay, TM0077 hydrolyzes acetate at positions 2, 3 and 4 with equal efficiencyas substrates in a ?-xylosidase-coupled assay
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
7-amino-cephalosporanic acid + H2O
7-amino-3-deacetylcephalosporanic acid + acetate
-
-
-
?
7-aminocephalosporanic acid + H2O
7-amino-3-deacetylcephalosporanic acid + acetate
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
7-aminocephalosporanic acid + H2O
deacetyl 7-aminocephalosporanic acid + acetate
alpha-ketoadipinyl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanic acid + alpha-ketoadipate
-
-
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
benzylcephalosporin + H2O
acetate + deacetylbenzylcephalosporin
benzyloxycarbonyl-7-aminocephalosporanic acid + H2O
?
cephaloglycin + H2O
acetate + (6R,7R)-7-{[(2R)-2-amino-2-phenylacetyl]amino}-3-(hydroxymethyl)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
cephalosporin C + H2O
deacetylcephalosporin C + acetate
cephalothin + H2O
acetate + deacetylcephalothin
cephapirin + H2O
acetate + deacetylcephapirin
D-glucose pentaacetate + H2O
?
-
-
-
?
D-glucose pentaacetate + H2O
D-glucose + acetate
D-xylose tetraacetate + H2O
?
-
-
-
?
D-xylose tetraacetate + H2O
D-xylose + acetate
-
-
-
?
deacetyl-7-aminocephalosporanic acid + ethyl acetate
7-aminocephalosporanic acid + ethanol
-
-
-
?
deacetyl-7-aminocephalosporanic acid + ethylene glycol diacetate
7-aminocephalosporanic acid + ?
deacetyl-7-aminocephalosporanic acid + isopropenyl acetate
7-aminocephalosporanic acid + ?
-
-
-
?
deacetyl-7-aminocephalosporanic acid + methyl acetate
7-aminocephalosporanic acid + methanol
-
-
-
?
ethyl acetate + H2O2
ethanol + peracetic acid
-
-
-
?
fluorescein di(acetoxymethyl ether) + H2O
?
-
-
-
?
fluorescein dibutyloxymethyl ether + H2O
?
-
-
-
?
fluorescein dicaproyloxymethyl ether + H2O
?
-
-
-
?
fluorescein dipropanoyloxymethyl ether + H2O
?
-
-
-
?
fluorescein dipropyloxymethyl ether + H2O
?
fluorescein divaleryloxymethyl ether + H2O
?
-
-
-
?
glucose pentaacetate + H2O
?
glucose pentaacetate + H2O
? + acetate
-
-
-
?
glucose pentacetate + H2O
?
-
-
-
?
glutaryl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanic acid + glutamate
glycerol triacetate + H2O2
glycerol diacetate + peracetic acid
-
-
-
?
monoacetin + H2O
acetate + glycerol
-
-
-
-
?
monochloroacetyl-7-aminocephalosporanic acid + H2O
acetate + monochloroacetyl-deacetyl-7-aminocephalosporanic acid
p-nitrophenyl acetate + H2O
4-nitrophenol + acetate
phenoxymethylcephalosporin + H2O
acetate + deacetylphenoxycephalosporin
tetraacetylxylose + H2O
?
-
-
-
?
xylose tetraacetate + H2O
? + acetate
-
-
-
?
additional information
?
-
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) bis(1-methylcyclopropane-1-carboxylate) + H2O
?
-
-
-
?
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) bis(1-methylcyclopropane-1-carboxylate) + H2O
?
-
-
-
?
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) bis(2-methylacrylate) + H2O
?
-
-
-
?
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) bis(2-methylacrylate) + H2O
?
-
-
-
?
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) dicyclobutanecarboxylate + H2O
?
-
-
-
?
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) dicyclobutanecarboxylate + H2O
?
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
?
2-(2-oxo-1,3-dihydroindol-3-yl) acetic acid + H2O
?
-
-
-
?
2-(2-oxo-1,3-dihydroindol-3-yl) acetic acid + H2O
?
-
-
-
?
2-(2-oxo-1,3-dihydroindol-3-yl) acetic acid + H2O
?
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
7-aminocephalosporanic acid + H2O
7-amino-3-deacetylcephalosporanic acid + acetate
-
colorimetric assay method development using bromothymol blue, validation, overview
-
-
?
7-aminocephalosporanic acid + H2O
7-amino-3-deacetylcephalosporanic acid + acetate
-
colorimetric assay method development using bromothymol blue, validation, overview
-
-
?
7-aminocephalosporanic acid + H2O
7-amino-3-deacetylcephalosporanic acid + acetate
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
Citrus sp.
-
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
7-aminocephalosporanic acid + H2O
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
7-aminocephalosporanic acid + H2O
deacetyl 7-aminocephalosporanic acid + acetate
-
-
reaction product is not less than 97.5% pure, only a negligible amount of deacetyl 7-aminocephalospornolactone detected
-
?
7-aminocephalosporanic acid + H2O
deacetyl 7-aminocephalosporanic acid + acetate
-
-
reaction product is not less than 97.5% pure, only a negligible amount of deacetyl 7-aminocephalospornolactone detected
-
?
7-aminocephalosporanic acid + H2O
deacetyl 7-aminocephalosporanic acid + acetate
-
-
-
?
7-aminocephalosporanic acid + H2O
deacetyl 7-aminocephalosporanic acid + acetate
-
-
-
?
7-aminocephalosporanic acid + H2O
deacetyl 7-aminocephalosporanic acid + acetate
-
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
benzylcephalosporin + H2O
acetate + deacetylbenzylcephalosporin
-
i.e. 7-(phenylacetamido)-cephalosporanic acid
-
-
?
benzylcephalosporin + H2O
acetate + deacetylbenzylcephalosporin
-
i.e. 7-(phenylacetamido)-cephalosporanic acid
-
-
?
benzyloxycarbonyl-7-aminocephalosporanic acid + H2O
?
-
-
-
-
?
benzyloxycarbonyl-7-aminocephalosporanic acid + H2O
?
-
-
-
-
?
cephaloglycin + H2O
acetate + (6R,7R)-7-{[(2R)-2-amino-2-phenylacetyl]amino}-3-(hydroxymethyl)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
-
-
?
cephaloglycin + H2O
acetate + (6R,7R)-7-{[(2R)-2-amino-2-phenylacetyl]amino}-3-(hydroxymethyl)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
-
-
?
cephaloglycin + H2O
acetate + (6R,7R)-7-{[(2R)-2-amino-2-phenylacetyl]amino}-3-(hydroxymethyl)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
colorimetric assay method development using bromothymol blue, validation, overview
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
colorimetric assay method development using bromothymol blue, validation, overview
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
Citrus sp.
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
last step in the cephalosporin C biosynthetic pathway
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
reaction using the recombinant Acremonium chrysogenum strain scaled up to a 4.000 l fermentor
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
-
-
-
?
cephalothin + H2O
acetate + deacetylcephalothin
-
-
-
-
?
cephalothin + H2O
acetate + deacetylcephalothin
-
-
-
-
?
cephalothin + H2O
acetate + deacetylcephalothin
-
-
-
-
?
cephalothin + H2O
acetate + deacetylcephalothin
-
-
-
-
?
cephalothin + H2O
acetate + deacetylcephalothin
Citrus sp.
-
-
-
-
?
cephalothin + H2O
acetate + deacetylcephalothin
-
i.e. 7-(thiophene-2-acetamido)-cephalosporanic acid
-
-
?
cephalothin + H2O
acetate + deacetylcephalothin
-
i.e. 7-(thiophene-2-acetamido)-cephalosporanic acid
-
-
?
cephapirin + H2O
acetate + deacetylcephapirin
-
-
-
-
?
cephapirin + H2O
acetate + deacetylcephapirin
-
-
-
-
?
cephapirin + H2O
acetate + deacetylcephapirin
-
-
-
-
?
D-glucose pentaacetate + H2O
D-glucose + acetate
-
-
-
?
D-glucose pentaacetate + H2O
D-glucose + acetate
-
-
-
?
D-glucose pentaacetate + H2O
D-glucose + acetate
-
-
-
?
deacetyl-7-aminocephalosporanic acid + ethylene glycol diacetate
7-aminocephalosporanic acid + ?
-
-
-
?
deacetyl-7-aminocephalosporanic acid + ethylene glycol diacetate
7-aminocephalosporanic acid + ?
-
-
-
?
fluorescein dipropyloxymethyl ether + H2O
?
-
-
-
?
fluorescein dipropyloxymethyl ether + H2O
?
-
-
-
?
fluorescein dipropyloxymethyl ether + H2O
?
-
-
-
?
glucose pentaacetate + H2O
?
-
-
-
-
?
glucose pentaacetate + H2O
?
-
-
-
-
?
glutaryl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanic acid + glutamate
-
-
-
-
?
glutaryl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanic acid + glutamate
-
-
-
-
?
monochloroacetyl-7-aminocephalosporanic acid + H2O
acetate + monochloroacetyl-deacetyl-7-aminocephalosporanic acid
-
-
-
-
?
monochloroacetyl-7-aminocephalosporanic acid + H2O
acetate + monochloroacetyl-deacetyl-7-aminocephalosporanic acid
-
-
-
?
monochloroacetyl-7-aminocephalosporanic acid + H2O
acetate + monochloroacetyl-deacetyl-7-aminocephalosporanic acid
-
-
-
-
?
p-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
phenoxymethylcephalosporin + H2O
acetate + deacetylphenoxycephalosporin
-
i.e. 7-(phenoxyacetamido)-cephalosporanic acid
-
-
?
phenoxymethylcephalosporin + H2O
acetate + deacetylphenoxycephalosporin
-
i.e. 7-(phenoxyacetamido)-cephalosporanic acid
-
-
?
triacetin + H2O
?
-
-
-
-
?
triacetin + H2O
?
-
-
-
-
?
triacetin + H2O
?
Citrus sp.
-
-
-
-
?
additional information
?
-
-
addition of glucose, maltose, and sucrose to the culture broth suppresses the enzyme production
-
-
?
additional information
?
-
-
no substrate: cephamycin C
-
?
additional information
?
-
-
no substrate: cephamycin C
-
?
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
-
-
?
additional information
?
-
the enzyme hydrolyzes the ester linkages of the acetyl groups in both the xylose moieties of the acetylated xylan fragments
-
-
?
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
-
-
?
additional information
?
-
the enzyme hydrolyzes the ester linkages of the acetyl groups in both the xylose moieties of the acetylated xylan fragments
-
-
?
additional information
?
-
the enzyme is active on a variety of acetylated compounds, including cephalosporin C, its esterase activity is confined to short-chain acyl esters of C2-C3 chain length
-
-
?
additional information
?
-
the enzyme is an acetyl esterase and not an acetyl xylan esterase, that shows no activity with xylan or acetylated xylan
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00054
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) bis(1-methylcyclopropane-1-carboxylate)
pH 7.3, 25°C
0.00051
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) bis(2-methylacrylate)
pH 7.3, 25°C
0.00096
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) dicyclobutanecarboxylate
pH 7.3, 25°C
0.148 - 0.197
4-methylumbelliferyl acetate
0.175 - 0.76
4-nitrophenyl acetate
1.12 - 20.8
7-aminocephalosporanic acid
1.11
benzyloxycarbonyl-7-aminocephalosporanic acid
-
-
4.7 - 215
cephalosporin C
409.1
ethyl acetate
free enzyme, pH 6.5, 25°C
0.0037
fluorescein di(acetoxymethyl ether)
pH 7.3, 25°C
0.00041
fluorescein dibutyloxymethyl ether
pH 7.3, 25°C
0.0026
fluorescein dicaproyloxymethyl ether
pH 7.3, 25°C
0.00097
fluorescein dipropanoyloxymethyl ether
pH 7.3, 25°C
0.001
fluorescein divaleryloxymethyl ether
pH 7.3, 25°C
0.203 - 0.224
Glucose pentaacetate
140.7 - 315.3
glycerol triacetate
2.03
monochloroacetyl-7-aminocephalosporanic acid
-
-
1
p-nitrophenyl acetate
-
-
0.059 - 0.189
xylose tetraacetate
additional information
additional information
-
kinetics
-
0.148
4-methylumbelliferyl acetate
wild-type including expression and purification tag, pH 8.0, 50°C
0.175
4-methylumbelliferyl acetate
mutant lacking 4 amino acids at N-terminus, pH 8.0, 50°C
0.187
4-methylumbelliferyl acetate
mutant lacking 10 amino acids at N-terminus, pH 8.0, 50°C
0.197
4-methylumbelliferyl acetate
wild-type, pH 8.0, 50°C
0.175
4-nitrophenyl acetate
wild-type including expression and purification tag, pH 8.0, 50°C
0.193
4-nitrophenyl acetate
wild-type, pH 8.0, 50°C
0.231
4-nitrophenyl acetate
mutant lacking 4 amino acids at N-terminus, pH 8.0, 50°C
0.309
4-nitrophenyl acetate
mutant lacking 10 amino acids at N-terminus, pH 8.0, 50°C
0.76
4-nitrophenyl acetate
pH 7.3, 25°C
1.12
7-aminocephalosporanic acid
mutant lacking 4 amino acids at N-terminus, pH 8.0, 50°C
1.135
7-aminocephalosporanic acid
wild-type, pH 8.0, 50°C
1.384
7-aminocephalosporanic acid
wild-type including expression and purification tag, pH 8.0, 50°C
1.43
7-aminocephalosporanic acid
-
-
1.563
7-aminocephalosporanic acid
mutant lacking 10 amino acids at N-terminus, pH 8.0, 50°C
2.8
7-aminocephalosporanic acid
-
-
6.5
7-aminocephalosporanic acid
-
strain ATCC6633
7.4
7-aminocephalosporanic acid
-
recombinant enzyme, 30°C
7.9
7-aminocephalosporanic acid
-
strain SHS 0133, FERM BP-2755
8.3
7-aminocephalosporanic acid
-
pH 8, 37°C
20.8
7-aminocephalosporanic acid
pH 7.3, 25°C
9.2
cephaloglycin
-
recombinant enzyme
4.7
cephalosporin C
Citrus sp.
-
-
7
cephalosporin C
-
pH 8, 37°C
33.7
cephalosporin C
-
pH 8, 37°C
34.5
cephalosporin C
-
recombinant enzyme
215
cephalosporin C
-
pH 7.3, 25°C, recombinant enzyme
8.6
cephalotin
Citrus sp.
-
-
11.7
cephalotin
-
recombinant enzyme
13.9
cephapirin
-
-
16.7
cephapirin
-
recombinant enzyme
0.203
Glucose pentaacetate
mutant lacking 4 amino acids at N-terminus, pH 8.0, 50°C
0.207
Glucose pentaacetate
mutant lacking 10 amino acids at N-terminus, pH 8.0, 50°C
0.207
Glucose pentaacetate
wild-type including expression and purification tag, pH 8.0, 50°C
0.224
Glucose pentaacetate
wild-type, pH 8.0, 50°C
140.7
glycerol triacetate
free enzyme, pH 6.5, 25°C
315.3
glycerol triacetate
immobilized enzyme, pH 6.5, 25°C
1.1
H2O2
free enzyme, pH 6.5, 25°C
1.15
H2O2
immobilized enzyme, pH 6.5, 25°C
0.46
Triacetin
-
-
30 - 32
Triacetin
Citrus sp.
-
-
0.059
xylose tetraacetate
mutant lacking 10 amino acids at N-terminus, pH 8.0, 50°C
0.134
xylose tetraacetate
mutant lacking 4 amino acids at N-terminus, pH 8.0, 50°C
0.134
xylose tetraacetate
wild-type including expression and purification tag, pH 8.0, 50°C
0.189
xylose tetraacetate
wild-type, pH 8.0, 50°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0046
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) bis(1-methylcyclopropane-1-carboxylate)
pH 7.3, 25°C
0.14
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) bis(2-methylacrylate)
pH 7.3, 25°C
0.023
((3-oxo-3H-spiro[isobenzofuran-1,9'-xanthene]-3',6'-diyl)bis(oxy))bis(methylene) dicyclobutanecarboxylate
pH 7.3, 25°C
171 - 320
4-methylumbelliferyl acetate
23 - 497
4-nitrophenyl acetate
0.83 - 21
7-aminocephalosporanic acid
0.089
ethyl acetate
free enzyme, pH 6.5, 25°C
14.1
fluorescein di(acetoxymethyl ether)
pH 7.3, 25°C
0.015
fluorescein dibutyloxymethyl ether
pH 7.3, 25°C
0.14
fluorescein dicaproyloxymethyl ether
pH 7.3, 25°C
6.4
fluorescein dipropanoyloxymethyl ether
pH 7.3, 25°C
0.004
fluorescein divaleryloxymethyl ether
pH 7.3, 25°C
1418 - 1558
Glucose pentaacetate
0.4 - 2.53
glycerol triacetate
1725 - 2866
xylose tetraacetate
171
4-methylumbelliferyl acetate
mutant lacking 10 amino acids at N-terminus, pH 8.0, 50°C
228
4-methylumbelliferyl acetate
mutant lacking 4 amino acids at N-terminus, pH 8.0, 50°C
289
4-methylumbelliferyl acetate
wild-type including expression and purification tag, pH 8.0, 50°C
320
4-methylumbelliferyl acetate
wild-type, pH 8.0, 50°C
23
4-nitrophenyl acetate
pH 7.3, 25°C
155
4-nitrophenyl acetate
mutant lacking 10 amino acids at N-terminus, pH 8.0, 50°C
211
4-nitrophenyl acetate
mutant lacking 4 amino acids at N-terminus, pH 8.0, 50°C
344
4-nitrophenyl acetate
wild-type including expression and purification tag, pH 8.0, 50°C
497
4-nitrophenyl acetate
wild-type, pH 8.0, 50°C
0.83
7-aminocephalosporanic acid
pH 7.3, 25°C
9
7-aminocephalosporanic acid
mutant lacking 10 amino acids at N-terminus, pH 8.0, 50°C
18
7-aminocephalosporanic acid
mutant lacking 4 amino acids at N-terminus, pH 8.0, 50°C
18
7-aminocephalosporanic acid
wild-type including expression and purification tag, pH 8.0, 50°C
21
7-aminocephalosporanic acid
wild-type, pH 8.0, 50°C
1418
Glucose pentaacetate
mutant lacking 10 amino acids at N-terminus, pH 8.0, 50°C
1456
Glucose pentaacetate
mutant lacking 4 amino acids at N-terminus, pH 8.0, 50°C
1555
Glucose pentaacetate
wild-type, pH 8.0, 50°C
1558
Glucose pentaacetate
wild-type including expression and purification tag, pH 8.0, 50°C
0.4
glycerol triacetate
immobilized enzyme, pH 6.5, 25°C
2.53
glycerol triacetate
free enzyme, pH 6.5, 25°C
1.09
H2O2
immobilized enzyme, pH 6.5, 25°C
3.3
H2O2
free enzyme, pH 6.5, 25°C
1725
xylose tetraacetate
wild-type, pH 8.0, 50°C
1994
xylose tetraacetate
mutant lacking 4 amino acids at N-terminus, pH 8.0, 50°C
2083
xylose tetraacetate
wild-type including expression and purification tag, pH 8.0, 50°C
2866
xylose tetraacetate
mutant lacking 10 amino acids at N-terminus, pH 8.0, 50°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1086
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-methylumbelliferyl acetate
1245
purified recombinant enzyme, pH 7.0, 40°C, substrate glucose pentacetate
16.81
substrate: 1-naphthyl acetate, pH 8.0, 50°C, wild-type enzyme
16.91
with 1-naphthyl acetate as substrate, wild type enzyme, at pH 8.0 and 50°C
187.4
-
hydrolysis of p-nitrophenyl acetate
2.72
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-nitrophenyl butyrate
2949
purified recombinant enzyme, pH 7.0, 40°C, substrate 4-nitrophenyl acetate
741
purified recombinant enzyme, pH 7.0, 40°C, substrate alpha-naphthyl acetate
962
purified recombinant enzyme, pH 7.0, 40°C, substrate beta-naphthyl acetate
0.075
substrate: 7-aminocephalosporanic acid, pH 8.0, 50°C, mutant enzyme P228A
0.075
with 7-amino-cephalosporanic acid as substrate, mutant enzyme P228A, at pH 8.0 and 50°C
0.47
substrate: 1-naphthyl acetate, pH 8.0, 50°C, mutant enzyme P228A
0.47
with 1-naphthyl acetate as substrate, mutant enzyme P228A, at pH 8.0 and 50°C
1.78
substrate: 4-nitrophenyl acetate, pH 8.0, 50°C, mutant enzyme P228A
1.78
with 4-nitrophenyl acetate as substrate, mutant enzyme P228A, at pH 8.0 and 50°C
10
substrate: 7-aminocephalosporanic acid, pH 8.0, 50°C, wild-type enzyme
10
with 7-amino-cephalosporanic acid as substrate, wild type enzyme, at pH 8.0 and 50°C
25.31
substrate: D-glucose pentaacetate, pH 8.0, 50°C, mutant enzyme P228A
25.31
with D-glucose pentaacetate as substrate, mutant enzyme P228A, at pH 8.0 and 50°C
29.8
substrate: D-xylose tetraacetate, pH 8.0, 50°C, mutant enzyme P228A
29.8
with D-xylose tetraacetate as substrate, mutant enzyme P228A, at pH 8.0 and 50°C
3.98
substrate: 4-methylumbelliferyl acetate, pH 8.0, 50°C, mutant enzyme P228A
3.98
with 4-methylumbelliferyl acetate as substrate, mutant enzyme P228A, at pH 8.0 and 50°C
346.22
substrate: D-xylose tetraacetate, pH 8.0, 50°C, wild-type enzyme
346.22
with D-xylose tetraacetate as substrate, wild type enzyme, at pH 8.0 and 50°C
41.49
substrate: 4-methylumbelliferyl acetate, pH 8.0, 50°C, wild-type enzyme
41.49
with 4-methylumbelliferyl acetate as substrate, wild type enzyme, at pH 8.0 and 50°C
415.5
substrate: D-glucose pentaacetate, pH 8.0, 50°C, wild-type enzyme
415.5
with D-glucose pentaacetate as substrate, wild type enzyme, at pH 8.0 and 50°C
49.33
substrate: 4-nitrophenyl acetate, pH 8.0, 50°C, wild-type enzyme
49.33
with 4-nitrophenyl acetate as substrate, wild type enzyme, at pH 8.0 and 50°C
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
synthesis
synthesis of peracetic acid. Recombinant enzyme can be efficiently produced in a low-cost autoinduction medium with an activity of 6800 U/ml. Optimal synthesis of peracetic is achieved with 0.30 mg/ml crude enzyme, 300 mM glycerol triacetate, and 1 M hydrogen peroxide, pH 8.0, and 2°C, which produces approximately 150 mM of peracetic acid within 5 min. When immobilized on an acrylate amino resin, the activity of the immobilized enzyme is 383.7 U/g
S188A
active site knockout
S188A
-
active site knockout
-
P228A
the mutation does not affect the overall secondary, tertiary, and quaternary structures and moderately decreases the thermal stability. However, the wild type cis conformation of the 227-228 peptide bond adopts a trans conformation in the variant. The results suggest that the conserved proline residue is responsible for the cis conformation of the peptide and shapes the geometry of the active site. Elimination of the pyrrolidine ring results in the loss of van der Waals and hydrophobic interactions with both the alcohol and acyl moeities of the ester substrate, leading to significant impairment of the activity and perturbation of substrate specificity
P228A
the mutation does not affect the overall secondary, tertiary, and quaternary structures, but has a significantly decreasing effect on the activity and moderately decreases the thermal stability of the enzyme. The wild type cis conformation of the 227-228 peptide bond adopts a trans conformation in the variant
P228A
-
the mutation does not affect the overall secondary, tertiary, and quaternary structures and moderately decreases the thermal stability. However, the wild type cis conformation of the 227-228 peptide bond adopts a trans conformation in the variant. The results suggest that the conserved proline residue is responsible for the cis conformation of the peptide and shapes the geometry of the active site. Elimination of the pyrrolidine ring results in the loss of van der Waals and hydrophobic interactions with both the alcohol and acyl moeities of the ester substrate, leading to significant impairment of the activity and perturbation of substrate specificity
-
P228A
-
the mutation does not affect the overall secondary, tertiary, and quaternary structures, but has a significantly decreasing effect on the activity and moderately decreases the thermal stability of the enzyme. The wild type cis conformation of the 227-228 peptide bond adopts a trans conformation in the variant
-
P228A
-
the mutation does not affect the overall secondary, tertiary, and quaternary structures and moderately decreases the thermal stability. However, the wild type cis conformation of the 227-228 peptide bond adopts a trans conformation in the variant. The results suggest that the conserved proline residue is responsible for the cis conformation of the peptide and shapes the geometry of the active site. Elimination of the pyrrolidine ring results in the loss of van der Waals and hydrophobic interactions with both the alcohol and acyl moeities of the ester substrate, leading to significant impairment of the activity and perturbation of substrate specificity
-
P228A
-
the mutation does not affect the overall secondary, tertiary, and quaternary structures, but has a significantly decreasing effect on the activity and moderately decreases the thermal stability of the enzyme. The wild type cis conformation of the 227-228 peptide bond adopts a trans conformation in the variant
-
additional information
-
construction of beta-lactamase (AmpC) and cephalosporin acetyl esterase (Aes) single or double knockout mutant strains from Escherichia coli strains JM105 and JM109(DE3), the chromosomal genes ampC and aes are disrupted by the phage lambda red recombinase system, which involves three stepswith three helper plasmids pKD13, pKD46 and pCP20, single or double knockout of ampC and aes from Escherichia coli JM105 have minimal effects on formal growth of the recombinant cells. Recombinant expression of Pseudomonas sp. strain SE83 cephalosporin C acylase II (sCPCAcy), EC 3.5.1.93, from vector pMKC-sCPCacy restores the cephalosporin C decomposition activity to an even higher level compared to wild-type, overview. CPC acylase II catalyzes a one-step enzymatic conversion of cephalosporin C into 7-aminocephalosporanic acid
additional information
-
construction of beta-lactamase (AmpC) and cephalosporin acetyl esterase (Aes) single or double knockout mutant strains from Escherichia coli strains JM105 and JM109(DE3), the chromosomal genes ampC and aes are disrupted by the phage lambda red recombinase system, which involves three stepswith three helper plasmids pKD13, pKD46 and pCP20, single or double knockout of ampC and aes from Escherichia coli JM105 have minimal effects on formal growth of the recombinant cells. Recombinant expression of Pseudomonas sp. strain SE83 cephalosporin C acylase II (sCPCAcy), EC 3.5.1.93, from vector pMKC-sCPCacy restores the cephalosporin C decomposition activity to an even higher level compared to wild-type, overview. CPC acylase II catalyzes a one-step enzymatic conversion of cephalosporin C into 7-aminocephalosporanic acid
-
additional information
construction of truncation variants lacking four and ten residues of the N-terminal region. The truncations do not affect the secondary structure or the fold but modulate the oligomerization dynamics. A modest in substrate specificity for acetylated xylose is observed compared with acetylated glucose. Variants show a drastic reduction of 30-40°C in the optimum temperature for activity
additional information
-
construction of truncation variants lacking four and ten residues of the N-terminal region. The truncations do not affect the secondary structure or the fold but modulate the oligomerization dynamics. A modest in substrate specificity for acetylated xylose is observed compared with acetylated glucose. Variants show a drastic reduction of 30-40°C in the optimum temperature for activity
-
additional information
-
construction of truncation variants lacking four and ten residues of the N-terminal region. The truncations do not affect the secondary structure or the fold but modulate the oligomerization dynamics. A modest in substrate specificity for acetylated xylose is observed compared with acetylated glucose. Variants show a drastic reduction of 30-40°C in the optimum temperature for activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Singh, K.; Sun, S.; Rakhit, S.
Cephalosporin acetylesterase activity of Fusaria
Eur. J. Appl. Microbiol. Biotechnol.
9
15-18
1980
Fusarium oxysporum, Fusarium oxysporum AY F-298
-
brenda
Abbott, B.J.; Cerimele, B.; Fukuda, D.S.
Immobilization of a cephalosporin acetylesterase by containment within an ultrafiltration device
Biotechnol. Bioeng.
18
1033-1042
1976
Bacillus subtilis
brenda
Hinnem, A.; Nuesch, J.
Enzymatic hydrolysis of cephalosporin C by an extracellular acetylhydrolase of Cephalosporium acremonium
Antimicrob. Agents Chemother.
9
824-830
1976
Acremonium chrysogenum
brenda
Abbott, B.J.; Fukuda, D.S.
Physical properties and kinetic behavior of a cephalosporin acetylesterase produced by Bacillus subtilis
Appl. Microbiol.
30
413-419
1975
Bacillus subtilis
brenda
Abbott, B.J.; Fukuda, D.S.
Cephalosporin acetylesterase (Bacillus subtilis)
Methods Enzymol.
43
731-734
1978
Bacillus subtilis, Bacillus subtilis WRRL-B-558
brenda
Abraham, E.P.; Fawcett, P.
Cephalosporin acetylesterase (citrus)
Methods Enzymol.
43
728-731
1975
Citrus sp.
brenda
Fujisawa, Y.; Shirafuji, H.; Kanzaki, T.
Deacetylcephalosporin C formation by cephalosporin C acetylhydrolase induced in a Cephalosporium acremonium
Agric. Biol. Chem.
39
1303-1309
1975
Acremonium chrysogenum
-
brenda
Nuesch, J.; Hinnen, A.; Liersch, M.; Treichler, H.J.
A biochemical and genetical approach to the biosynthesis of cephalosporin C
Proc. Int. Symp. Genet. Ind. Microorg. (McDonald, K. D. , ed. )
451-472
1976
Acremonium chrysogenum
-
brenda
Fujisawa, Y.; Shirafuji, H.; Kida, M.; Nara, K.
New findings on cephalosporin C biosynthesis
Nature New Biol.
246
154-155
1973
Acremonium chrysogenum
brenda
Sakai, Y.; Abe, T.; Aoki, M.; Ohabayashi, Y.; Yamamoto, K.; Tani, Y.; Kato, N.
Purification and properties of cephalosporin-C deacetylase from the yeast, Rhodotorula glutinis 38B1, useful for bioconversion of 7-aminocephalosporanic acid derivatives
J. Ferment. Bioeng.
85
53-57
1998
Rhodotorula glutinis, Rhodotorula glutinis 38B1
-
brenda
Takimoto, A.; Mitsushima, K.; Yagi, S.; Sonoyama, T.
Purification, characterization and partial amino acid sequences of a novel cephalosporin-C deacetylase from Bacillus subtilis
J. Ferment. Bioeng.
77
17-22
1994
Bacillus subtilis, Bacillus subtilis ATCC 6633, Bacillus subtilis SHS 0133
-
brenda
Mitsushima, K.; Takimoto, A.; Sonoyama, T.; Yagi, S.
Gene cloning, nucleotide sequence, and expression of a cephalosporin-C deacetylase from Bacillus subtilis
Appl. Environ. Microbiol.
61
2224-2229
1995
Bacillus subtilis, Bacillus subtilis SHS 0133
brenda
Politino, M.; Tonzi, S.M.; Burnett, W.V.; Romancik, G.; Usher, J.J.
Purification and characterization of a cephalosporin esterase from Phodosporidium toruloides
Appl. Environ. Microbiol.
63
4807-4811
1997
Bacillus subtilis, Rhodotorula toruloides
brenda
Sakai, Y.; Abe, T.; Ohbayashi, Y.; Isaka, K.; Yamamoto, K.; Tani, Y.; Kato, N.
Bioconversion of 7-aminocephalosporanic acid by intact Rhodotorula glutinis cells
Appl. Environ. Microbiol.
62
2669-2672
1996
Rhodotorula glutinis
brenda
Takimoto, A.; Yagi, S.; Mitsushima, K.
High-level expression, purification, and some properties of a recombinant cephalosporin-C deacetylase
J. Biosci. Bioeng.
87
456-462
1999
Bacillus subtilis, Bacillus subtilis SHS 0133
brenda
Cardoza, R.E.; Velasco, J.; Martin, J.F.; Liras, P.
A cephalosporin C acetylhydrolase is present in the cultures of Nocardia lactamdurans
Appl. Microbiol. Biotechnol.
54
406-412
2000
Amycolatopsis lactamdurans, Amycolatopsis lactamdurans MA4213
brenda
Velasco, J.; Gutierrez, S.; Casqueiro, J.; Fierro, F.; Campoy, S.; Martin, J.F.
Cloning and characterization of the gene cahB encoding a cephalosporin C acetylhydrolase from Acremonium chrysogenum
Appl. Microbiol. Biotechnol.
57
350-356
2001
Acremonium chrysogenum, Acremonium chrysogenum C10 / ATCC 48272
brenda
Lee, H.W.; Ko, J.Y.; Kim, W.J.; Byun, S.M.
Isolation, analysis, and expression of lipase with cephalosporin-C deacetylation activity from Staphylococcus sp
J. Biochem. Mol. Biol.
34
274-277
2001
Staphylococcus sp.
-
brenda
Vincent, F.; Charnock, S.J.; Verschueren, K.H.; Turkenburg, J.P.; Scott, D.J.; Offen, W.A.; Roberts, S.; Pell, G.; Gilbert, H.J.; Davies, G.J.; Brannigan, J.A.
Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9A resolution
J. Mol. Biol.
330
593-606
2003
Bacillus subtilis (P94388), Bacillus subtilis
brenda
Verweij, J.; Vroom, E.D.
Industrial transformation of penicillins and cephalosporins
Rec. Trav. Chim. Pays-Bas
112
66-81
1993
Escherichia coli, Pseudomonas sp., Pseudomonas sp. GK-16
-
brenda
Takimoto, A.; Takakura, T.; Tani, H.; Yagi, S.; Mitsushima, K.
Batch production of deacetyl 7-aminocephalosporanic acid by immobilized cephalosporin-C deacetylase
Appl. Microbiol. Biotechnol.
65
263-267
2004
Bacillus subtilis, Bacillus subtilis SHS0133
brenda
Basch, J.; Franceschini, T.; Tonzi, S.; Chiang, S.J.
Expression of a cephalosporin C esterase gene in Acremonium chrysogenum for the direct production of deacetylcephalosporin C
J. Ind. Microbiol. Biotechnol.
31
531-539
2004
Rhodotorula toruloides (O42728), Rhodotorula toruloides
brenda
Martinez-Martinez, I.; Montoro-Garcia, S.; Lozada-Ramirez, J.D.; Sanchez-Ferrer, A.; Garcia-Carmona, F.
A colorimetric assay for the determination of acetyl xylan esterase or cephalosporin C acetyl esterase activities using 7-amino cephalosporanic acid, cephalosporin C, or acetylated xylan as substrate
Anal. Biochem.
369
210-217
2007
Bacillus pumilus, Bacillus pumilus CECT 5072
brenda
Tian, Q.; Song, P.; Jiang, L.; Li, S.; Huang, H.
A novel cephalosporin deacetylating acetyl xylan esterase from Bacillus subtilis with high activity toward cephalosporin C and 7-aminocephalosporanic acid
Appl. Microbiol. Biotechnol.
98
2081-2089
2014
Bacillus subtilis (M1JUH6), Bacillus subtilis CICC 20034 (M1JUH6)
brenda
Wang, Y.; Yu, H.; Zhang, J.; Luo, H.; Shen, Z.
Double knockout of beta-lactamase and cephalosporin acetyl esterase genes from Escherichia coli reduces cephalosporin C decomposition
J. Biosci. Bioeng.
113
737-741
2012
Escherichia coli, Escherichia coli JM105
brenda
Levisson, M.; Han, G.W.; Deller, M.C.; Xu, Q.; Biely, P.; Hendriks, S.; Ten Eyck, L.F.; Flensburg, C.; Roversi, P.; Miller, M.D.; McMullan, D.; von Delft, F.; Kreusch, A.; Deacon, A.M.; van der Oost, J.; Lesley, S.A.; Elsliger, M.A.; Kengen, S.W.; Wilson, I.A.
Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima
Proteins
80
1545-1559
2012
Thermotoga maritima (Q9WXT2)
brenda
Singh, M.; Manoj, N.
Crystal structure of Thermotoga maritima acetyl esterase complex with a substrate analog Insights into the distinctive substrate specificity in the CE7 carbohydrate esterase family
Biochem. Biophys. Res. Commun.
476
63-68
2016
Thermotoga maritima (Q9WXT2), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9WXT2), Thermotoga maritima ATCC 43589 (Q9WXT2)
brenda
Hedge, M.; Gehring, A.; Adkins, C.; Weston, L.; Lavis, L.; Johnson, R.
The structural basis for the narrow substrate specificity of an acetyl esterase from Thermotoga maritima
Biochim. Biophys. Acta
1824
1024-1030
2012
Thermotoga maritima (Q9WXT2), Thermotoga maritima DSM 3109 (Q9WXT2)
brenda
Singh, M.; Manoj, N.
Structural role of a conserved active site cis proline in the Thermotoga maritima acetyl esterase from the carbohydrate esterase family 7
Proteins
85
694-708
2017
Thermotoga maritima (Q9WXT2), Thermotoga maritima DSM 3109 (Q9WXT2), Thermotoga maritima ATCC 43589 (Q9WXT2)
brenda
Ma, X.; Zhu, Y.; Sun, M.; Yang, S.; Su, E.; Wei, D.
High-level expression of Cephalosporin C deacetylase from Bacillus subtilis SIL3 in Escherichia coli by a multilevel collaborative strategy
Biochem. Eng. J.
114
183-190
2016
Bacillus subtilis, Bacillus subtilis SIL3
-
brenda
Ma, X.; Deng, S.; Su, E.; Wei, D.
One-pot enzymatic production of deacetyl-7-aminocephalosporanic acid from cephalosporin C via immobilized cephalosporin C acylase and deacetylase
Biochem. Eng. J.
95
1-8
2015
Pseudomonas sp. SE83
-
brenda
Tao, W.; Xu, Q.; Huang, H.; Li, S.
Efficient production of peracetic acid in aqueous solution with cephalosporin-deacetylating acetyl xylan esterase from Bacillus subtilis
Process Biochem.
50
2121-2127
2015
Bacillus subtilis (M1JUH6)
-
brenda