BRENDA - Enzyme Database show
show all sequences of 3.1.1.41

Purification and properties of cephalosporin-C deacetylase from the yeast, Rhodotorula glutinis 38B1, useful for bioconversion of 7-aminocephalosporanic acid derivatives

Sakai, Y.; Abe, T.; Aoki, M.; Ohabayashi, Y.; Yamamoto, K.; Tani, Y.; Kato, N.; J. Ferment. Bioeng. 85, 53-57 (1998)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
(p-amino-phenyl)methanesulfonyl fluoride
slight inhibition
Rhodotorula glutinis
5,5'-dithiobis(2-nitrobenzoate)
-
Rhodotorula glutinis
Cu2+
CuCl2
Rhodotorula glutinis
eserine sulfate
slight inhibition
Rhodotorula glutinis
Hg2+
HgCl2
Rhodotorula glutinis
PbCl2
-
Rhodotorula glutinis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.11
-
benzyloxycarbonyl-7-aminocephalosporanic acid
-
Rhodotorula glutinis
1.43
-
7-aminocephalosporanic acid
-
Rhodotorula glutinis
2.03
-
monochloroacetyl-7-aminocephalosporanic acid
-
Rhodotorula glutinis
8.39
-
cephalosporin C
-
Rhodotorula glutinis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cell wall
the majority of the enzyme is tightly bound to the cell wall
Rhodotorula glutinis
5618
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
82000
-
2 * 82000, SDS-PAGE
Rhodotorula glutinis
141000
-
gel filtration
Rhodotorula glutinis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodotorula glutinis
-
-
-
Rhodotorula glutinis 38B1
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
side-chain modification
N-linked sugar content is about 21% by weight
Rhodotorula glutinis
Purification (Commentary)
Commentary
Organism
-
Rhodotorula glutinis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
342
-
-
Rhodotorula glutinis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis 38B1
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
benzyloxycarbonyl-7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis
?
-
-
-
-
benzyloxycarbonyl-7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis 38B1
?
-
-
-
-
cephalosporin C + H2O
-
170672
Rhodotorula glutinis
deacetylcephalosporin C + acetate
-
170672
Rhodotorula glutinis
?
cephalosporin C + H2O
-
170672
Rhodotorula glutinis 38B1
deacetylcephalosporin C + acetate
-
170672
Rhodotorula glutinis 38B1
?
monochloroacetyl-7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis
acetate + monochloroacetyl-deacetyl-7-aminocephalosporanic acid
-
-
-
?
monochloroacetyl-7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis 38B1
acetate + monochloroacetyl-deacetyl-7-aminocephalosporanic acid
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 82000, SDS-PAGE
Rhodotorula glutinis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
35
-
-
Rhodotorula glutinis
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
10
45
10C: about 40% of maximal activity, 45C: about 30% of maximal activity
Rhodotorula glutinis
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
-
15 min, 60% loss of activity
Rhodotorula glutinis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
534
-
benzyloxycarbonyl-7-aminocephalosporanic acid
-
Rhodotorula glutinis
576
-
7-aminocephalosporanic acid
-
Rhodotorula glutinis
768
-
monochloroacetyl-7-aminocephalosporanic acid
-
Rhodotorula glutinis
1370
-
cephalosporin C
-
Rhodotorula glutinis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
-
-
Rhodotorula glutinis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4.2
7
pH 4.2: 30% of maximal activity, pH 7.0: about 35% of maximal activity
Rhodotorula glutinis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(p-amino-phenyl)methanesulfonyl fluoride
slight inhibition
Rhodotorula glutinis
5,5'-dithiobis(2-nitrobenzoate)
-
Rhodotorula glutinis
Cu2+
CuCl2
Rhodotorula glutinis
eserine sulfate
slight inhibition
Rhodotorula glutinis
Hg2+
HgCl2
Rhodotorula glutinis
PbCl2
-
Rhodotorula glutinis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.11
-
benzyloxycarbonyl-7-aminocephalosporanic acid
-
Rhodotorula glutinis
1.43
-
7-aminocephalosporanic acid
-
Rhodotorula glutinis
2.03
-
monochloroacetyl-7-aminocephalosporanic acid
-
Rhodotorula glutinis
8.39
-
cephalosporin C
-
Rhodotorula glutinis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cell wall
the majority of the enzyme is tightly bound to the cell wall
Rhodotorula glutinis
5618
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
82000
-
2 * 82000, SDS-PAGE
Rhodotorula glutinis
141000
-
gel filtration
Rhodotorula glutinis
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
side-chain modification
N-linked sugar content is about 21% by weight
Rhodotorula glutinis
Purification (Commentary) (protein specific)
Commentary
Organism
-
Rhodotorula glutinis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
342
-
-
Rhodotorula glutinis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis 38B1
acetate + deacetyl-7-aminocephalosporanic acid
-
-
-
?
benzyloxycarbonyl-7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis
?
-
-
-
-
benzyloxycarbonyl-7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis 38B1
?
-
-
-
-
cephalosporin C + H2O
-
170672
Rhodotorula glutinis
deacetylcephalosporin C + acetate
-
170672
Rhodotorula glutinis
?
cephalosporin C + H2O
-
170672
Rhodotorula glutinis 38B1
deacetylcephalosporin C + acetate
-
170672
Rhodotorula glutinis 38B1
?
monochloroacetyl-7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis
acetate + monochloroacetyl-deacetyl-7-aminocephalosporanic acid
-
-
-
?
monochloroacetyl-7-aminocephalosporanic acid + H2O
-
170672
Rhodotorula glutinis 38B1
acetate + monochloroacetyl-deacetyl-7-aminocephalosporanic acid
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 82000, SDS-PAGE
Rhodotorula glutinis
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
35
-
-
Rhodotorula glutinis
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
10
45
10C: about 40% of maximal activity, 45C: about 30% of maximal activity
Rhodotorula glutinis
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
-
15 min, 60% loss of activity
Rhodotorula glutinis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
534
-
benzyloxycarbonyl-7-aminocephalosporanic acid
-
Rhodotorula glutinis
576
-
7-aminocephalosporanic acid
-
Rhodotorula glutinis
768
-
monochloroacetyl-7-aminocephalosporanic acid
-
Rhodotorula glutinis
1370
-
cephalosporin C
-
Rhodotorula glutinis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
-
-
Rhodotorula glutinis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4.2
7
pH 4.2: 30% of maximal activity, pH 7.0: about 35% of maximal activity
Rhodotorula glutinis
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
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
749834
Ma
-
High-level expression of Ceph ...
Bacillus subtilis, Bacillus subtilis SIL3
Biochem. Eng. J.
114
183-190
2016
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
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-
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1
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
749837
Ma
-
One-pot enzymatic production ...
Pseudomonas sp. SE83
Biochem. Eng. J.
95
1-8
2015
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-
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-
1
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-
-
-
-
2
-
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-
-
-
-
-
-
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
-
-
1
1
-
-
-
-
2
-
5
-
-
1
-
-
-
-
1
4
-
-
-
1
-
-
-
2
-
-
-
-
-
1
1
-
-
-
1
-
1
-
-
-
-
-
2
-
-
-
1
-
-
-
1
4
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
675216
Basch
Expression of a cephalosporin ...
Rhodotorula toruloides
J. Ind. Microbiol. Biotechnol.
31
531-539
2004
-
1
1
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
652917
Vincent
Multifunctional xylooligosacch ...
Bacillus subtilis
J. Mol. Biol.
330
593-606
2003
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
649401
Velasco
Cloning and characterization o ...
Acremonium chrysogenum, Acremonium chrysogenum C10 / ATCC 48272
Appl. Microbiol. Biotechnol.
57
350-356
2001
-
-
-
-
-
-
2
1
1
-
2
-
-
7
-
1
1
-
-
-
-
-
4
-
1
1
-
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
1
1
-
2
-
-
-
1
1
-
-
-
-
4
-
1
1
-
-
1
1
-
1
-
-
-
-
-
-
651823
Lee
-
Isolation, analysis, and expre ...
Staphylococcus sp.
J. Biochem. Mol. Biol.
34
274-277
2001
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
1
1
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
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-
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649397
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A cephalosporin C acetylhydrol ...
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2000
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High-level expression, purific ...
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11
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5
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1
1
11
1
1
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1
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Sakai
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Purification and properties of ...
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6
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1
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8
1
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1
1
4
1
1
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170675
Politino
Purification and characterizat ...
Bacillus subtilis, Rhodotorula toruloides
Appl. Environ. Microbiol.
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4807-4811
1997
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1
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1
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7
1
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2
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170676
Sakai
Bioconversion of 7-aminocephal ...
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1996
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3
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170674
Mitsushima
Gene cloning, nucleotide seque ...
Bacillus subtilis, Bacillus subtilis SHS 0133
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2224-2229
1995
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1
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170673
Takimoto
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Purification, characterization ...
Bacillus subtilis, Bacillus subtilis ATCC 6633, Bacillus subtilis SHS 0133
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7
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7
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2
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4
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660484
Verweij
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Industrial transformation of p ...
Escherichia coli, Pseudomonas sp., Pseudomonas sp. GK-16
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1993
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170663
Singh
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Cephalosporin acetylesterase a ...
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1980
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Abbott
Cephalosporin acetylesterase ( ...
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12
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Abbott
Immobilization of a cephalospo ...
Bacillus subtilis
Biotechnol. Bioeng.
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1033-1042
1976
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170665
Hinnem
Enzymatic hydrolysis of cephal ...
Acremonium chrysogenum
Antimicrob. Agents Chemother.
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1976
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Nuesch
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Acremonium chrysogenum
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1976
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Abbott
Physical properties and kineti ...
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Abraham
Cephalosporin acetylesterase ( ...
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Fujisawa
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Deacetylcephalosporin C format ...
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Fujisawa
New findings on cephalosporin ...
Acremonium chrysogenum
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1973
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