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2 acetyl-CoA + chloramphenicol
2 CoA + chloramphenicol 1,3-diacetate
-
-
-
-
?
acetyl-CoA + 2-phenylethanol
CoA + 2-phenylethyl acetate
-
-
-
-
?
acetyl-CoA + benzyl alcohol
CoA + benzyl acetate
-
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
acetyl-CoA + chloramphenicol 1-acetate
CoA + chloramphenicol 1,3-diacetate
acetyl-CoA + D-threo-1-p-nitrophenyl-2-bromoacetamido-1,3-propanediol
CoA + ?
acetyl-CoA + D-threo-1-phenyl-2-dichloroacetamido-1,3-propanediol
CoA + ?
acetyl-CoA + isobutanol
CoA + isobutyl acetate
-
-
-
-
?
chloramphenicol + acetyl-CoA
chloramphenicol 3-acetate + CoA
-
-
-
?
additional information
?
-
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
inducible enzyme
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
inducible enzyme
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
in forward reaction formation of a ternary complex by a rapid-equilibrium mechanism, in reverse reaction rapid-equilibrium mechanism with random addition of substrates
-
r
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
catabolite repression of CAT synthesis is mediated by a mechanism involving cyclic adenosine 5'-monophosphate
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
inactivates chloramphenicol
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
enzymatic inactivation of chloramphenicol
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
all known R factors carrying the CAT gene in enteric bacteria mediate constitutive synthesis of the enzyme
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
in forward reaction formation of a ternary complex by a rapid-equilibrium mechanism, in reverse reaction rapid-equilibrium mechanism with random addition of substrates
-
r
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
acetylates only the biologically active D-threo stereoisomer
+ chloramphenicol 1,3-diacetate
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
inducible enzyme
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
inactivates chloramphenicol
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
acetylates only the biologically active D-threo stereoisomer
+ chloramphenicol 1,3-diacetate
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
inducible enzyme
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
inactivates chloramphenicol
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
inducible enzyme
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
inducible enzyme
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol
CoA + chloramphenicol 3-acetate
-
-
-
?
acetyl-CoA + chloramphenicol 1-acetate
CoA + chloramphenicol 1,3-diacetate
-
the enzyme acetylates specifically at the 3-hydroxy position. The diacetylation is possible only because of non-enzymatic interconversion of chloramphenical 3-acetate to chloramphenicol 1-acetate at higher pH values
-
?
acetyl-CoA + chloramphenicol 1-acetate
CoA + chloramphenicol 1,3-diacetate
-
no activity
-
-
?
acetyl-CoA + chloramphenicol 1-acetate
CoA + chloramphenicol 1,3-diacetate
-
no activity
-
-
?
acetyl-CoA + D-threo-1-p-nitrophenyl-2-bromoacetamido-1,3-propanediol
CoA + ?
-
-
-
-
?
acetyl-CoA + D-threo-1-p-nitrophenyl-2-bromoacetamido-1,3-propanediol
CoA + ?
-
-
-
-
?
acetyl-CoA + D-threo-1-p-nitrophenyl-2-bromoacetamido-1,3-propanediol
CoA + ?
-
-
-
-
?
acetyl-CoA + D-threo-1-phenyl-2-dichloroacetamido-1,3-propanediol
CoA + ?
-
-
-
-
?
acetyl-CoA + D-threo-1-phenyl-2-dichloroacetamido-1,3-propanediol
CoA + ?
-
-
-
-
?
acetyl-CoA + D-threo-1-phenyl-2-dichloroacetamido-1,3-propanediol
CoA + ?
-
-
-
-
?
additional information
?
-
-
a CAP derivative on sulfidic monolayers on gold chips can still serve as a substrate for the enzyme
-
-
?
additional information
?
-
-
poor substrates: butanol, propanol, ethanol, isopropanol. Specific ester production titers and rates are higher for aromatic alcohols than linear, short-chain alcohols
-
-
-
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A203G
-
mutant enzyme is less stable than wild-type enzyme
A203I
-
mutant enzyme is more thermostable than wild-type
I191V
-
mutant enzyme is less stable than wild-type enzyme
Y33F/A203V
-
mutant enzyme is more thermostable than wild-type
C214A
-
95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 31% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214D
-
50% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 85% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214E
-
75% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 84% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214F/G219S
-
95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 81% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214G
-
80% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 44% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214L
-
100% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 33% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214P
-
95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 88% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214Q
-
95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 73% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214R
-
55% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 84% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214S
-
95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 32% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214T
-
90% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 59% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214V
-
95% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 45% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
C214W
-
50% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 70% of activity after 30 min at 65 C compared to 15% for the wild-type enzyme
C214Y
-
90% of the in vivo produced mutant polypeptide is soluble compared to 90% for the wild-type enzyme. Mutant enzyme loses 81% of activity after 30 min at 65°C compared to 15% for the wild-type enzyme
CATIII (F24A/Y25F/L29A)
-
Km-value for acetyl-CoA is 0.095 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.023 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 30% of the wild-type enzyme CAT III
CATIII(K14E/H195A/K217A)
-
no activity
CATIII(Q92C/N146F/Y169F/I172V)
-
Km-value for acetyl-CoA is 0.165 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.02 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 60% of the wild-type enzyme CAT III
K14/K217E
-
Km-value for acetyl-CoA is 0.166 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.017 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 87% of the wild-type enzyme CAT III
L145F
-
folding of chloramphenicol acetyltransferase is hampered by deletion of the carboxy-terminal tail including the last residue of the carboxy-terminal alpha-helix. Such truncated CAT polypeptides quantitatively aggregate into cytoplasmic inclusion bodies, which results in absence of chloramphenicol-resistant phenotype for the producing host. Introduction of Phe at amino acid position 145 improves the ability of the protein to fold into a soluble, enzymatically active conformation
L158I
-
fluorinated mutant expressed in trifluoroleucine shows enhanced thermostability compared to CAT T (CAT expressed in trifluoroleucine), suggesting that trifluoroleucine at position 158 contributes to a portion of the observed loss in thermostability upon global fluorination. Relative activity: 89% (non-fluorinated mutant), 51.7% (fluorinated mutant)
L208I
-
fluorinated mutant expressed in trifluoroleucine shows loss in thermostability
L821I
-
fluorinated mutant expressed in trifluoroleucine shows loss in thermostability
[CATI (H195A)]2[CATIII(K14E/K217E)]
-
hybrid trimer, Km-value for acetyl-CoA is 0.072 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.018 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 14% of the wild-type enzyme CAT III
[CATIII]2[CATIII(K14E/H195A/K217A)]
-
Km-value for acetyl-CoA is 0.143 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.016 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 80% of the wild-type enzyme CAT III
[CATIII][CATIII(K14E/H195A/K217A)]2
-
Km-value for acetyl-CoA is 0.198 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.02 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 82% of the wild-type enzyme CAT III
[CATI][CATIII(K14E/H195A/K217E)]2
-
hybrid trimer, Km-value for acetyl-CoA is 0.107 mM compared to 0.093 mM for wild-type CATIII, Km-value for chloramphenicol is 0.02 mM compared to 0.012 mM for the wild-type CATIII, turnover number is 50% of the wild-type enzyme CAT III
G61S
-
G61S and Y105C contrtibute synergistically to the resistance phenotype of strain PAhcr1
G61S/Y105C
-
G61S and Y105C contrtibute synergistically to the resistance phenotype of strain PAhcr1
Y105C
-
G61S and Y105C contrtibute synergistically to the resistance phenotype of strain PAhcr1
G61S
-
G61S and Y105C contrtibute synergistically to the resistance phenotype of strain PAhcr1
-
G61S/Y105C
-
G61S and Y105C contrtibute synergistically to the resistance phenotype of strain PAhcr1
-
Y105C
-
G61S and Y105C contrtibute synergistically to the resistance phenotype of strain PAhcr1
-
A138S
-
site-directed mutagenesis, the enzyme mutant shows increased thermostability at 60-65°C for 24 h compared to the wild-type enzyme, thermostability enhancement results from the A138T replacement and can attributed to both the presence of a hydroxyl group and the bulk of the threonine side chain. CAT A138S mutation confers chloramphenicol resistance to Geobacillus kaustophilus cells at high temperature more efficiently than the wild-type enzyme
A138T
-
site-directed mutagenesis, the enzyme mutant shows increased thermostability at 60-65°C for 24 h compared to the wild-type enzyme, thermostability enhancement results from the A138T replacement and can attributed to both the presence of a hydroxyl group and the bulk of the threonine side chain. CAT A138T mutation confers chloramphenicol resistance to Geobacillus kaustophilus cells at high temperature more efficiently than the wild-type enzyme. The A138T substitution has no effect on CAT activity
A138V
-
site-directed mutagenesis, the enzyme mutant shows highly increased thermostability at 60-65°C for 24 h compared to the wild-type enzyme, thermostability enhancement results from the A138T replacement and can attributed to both the presence of a hydroxyl group and the bulk of the threonine side chain. CAT A138V mutation confers chloramphenicol resistance to Geobacillus kaustophilus cells at high temperature more efficiently than the wild-type enzyme
additional information
-
Bacillus subtilis cells expressing a hybrid protein (LvsSS-Cat) consisting of the Bacillus amyloliquefaciens levansucrose signal peptide fused to Bacillus pumilus chloramphenicol acetyltransferase are unable to export cat protein into the growth medium. A series of tripartite protein fusion is constructed by inserting various length of the cat sequences between the levansucrase signal peptide and staphylococcal protein A or Escherichia coli alkaline phosphatase. Biochemical characterization of the various Cat protein fusion reveales that multiple regions in the cat protein are causing the export defect
additional information
-
in soluble CATI(1-211)(X3) mutants nearly all amino acid residues are tolerated at position 212 and 213. This reflects the relative lack of impotance of these residues in the folding and/or stabilization of CAT. Substitutions at position 214 do not dramatically alter the biological activity of wild-type CATI
additional information
-
replacement of all the leucine residues in the enzyme chloramphenicol acetyltransferase with the analog, 5',5',5'-trifluoroleucine, results in the maintenance of enzymatic activity under ambient temperatures as well as an enhancement in secondary structure but loss in stability against heat and denaturants or organic co-solvents
additional information
-
residue-specific incorporation of T into chloramphenicol acetyltransferase (CAT) results in a loss of thermostability. Relative activity: 34.6% (fluorinated CAT)
additional information
-
thermoadaptation-directed enzyme evolution approach for generation of mutant genes encoding enzyme variants that are more thermostable than the parent enzyme using an error-prone thermophile strain MK480 derived from Geobacillus kaustophilus strain HTA426, increase of the thermostability of the chloramphenicol acetyltransferase (CAT) from Staphylococcus aureus and successfully generation of a CAT variant with an A138 replacement (CATA138X), method, overview
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Shaw, W.V.
The enzymatic acetylation of chloramphenicol by extracts of R factor-resistant Escherichia coli
J. Biol. Chem.
242
687-693
1967
Escherichia coli
brenda
Shaw, W.V.; Brodsky, R.F.
Characterization of chloramphenicol acetyltransferase from chloramphenicol-resistant Staphylococcus aureus
J. Bacteriol.
95
28-36
1968
Escherichia coli, Staphylococcus aureus, Staphylococcus aureus C22.1
brenda
Shaw, W.V.
Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria
Methods Enzymol.
43
737-755
1975
Agrobacterium tumefaciens, Streptococcus pneumoniae, Escherichia coli, Enterococcus faecalis, Staphylococcus sp.
brenda
Cardoso, M.; Schwarz, S.
Characterization of the chloramphenicol acetyltransferase variants encoded by the plasmids pSCS6 and pSCS7 from Staphylococcus aureus
J. Gen. Microbiol.
138
275-281
1992
Staphylococcus aureus
brenda
Roberts, M.; Corney, A.; Shaw, W.V.
Molecular characterization of three chloramphenicol acetyltransferases isolated from Haemophilus influenzae
J. Bacteriol.
151
737-741
1982
Haemophilus influenzae
brenda
Thibault, G.; Guitard, M.; Daigneault, R.
A study of the enzymatic inactivation of chloramphenicol by highly purified chloramphenicol acetyltransferase
Biochim. Biophys. Acta
614
339-349
1980
Escherichia coli
brenda
Masuyoshi, S.; Okubo, T.; Inoue, M.; Mitsuhashi, S.
Purification and some properties of a chloramphenicol acetyltransferase mediated by plasmids from Vibrio anguillarum
J. Biochem.
104
131-135
1988
Vibrio anguillarum
brenda
Murray, I.A.; Martinez-Suarez, J.V.; Close, T.J.; Shaw, W.V.
Nucleotide sequences of genes encoding the type II chloramphenicol acetyltransferases of Escherichia coli and Haemophilus influenzae, which are sensitive to inhibition by thiol-reactive reagents
Biochem. J.
272
505-510
1990
Escherichia coli, Haemophilus influenzae
brenda
Ellis, J.; Bagshaw, C.R.; Shaw, W.V.
Substrate binding to chloramphenicol acetyltransferase: evidence for negative cooperativity from equilibrium and kinetic constants for binary and ternary complexes
Biochemistry
30
10806-10813
1991
Escherichia coli
brenda
Zaidenzaig, Y.; Fitton, J.E.; Packman, L.C.; Shaw, W.V.
Characterization and comparison of chloramphenicol acetyltransferase variants
Eur. J. Biochem.
100
609-618
1979
Agrobacterium tumefaciens, Clostridium perfringens, Streptococcus pneumoniae, Haemophilus influenzae, Haemophilus parainfluenzae, Proteus mirabilis, Staphylococcus sp., Streptococcus agalactiae, Streptomyces acrimycini
brenda
Nolte, G.; Sussmuth, R.
Purification and characterization of chloramphenicol acetyltransferase from Flavobacterium CB60
J. Gen. Microbiol.
133
2115-2122
1987
Flavobacterium sp., Flavobacterium sp. CB60
brenda
Tanaka, H.; Izaki, K.; Takahashi, H.
Some properties of chloramphenicol acetyltransferase, with particular reference to the mechanism of inhibition by basic triphenylmethane dyes
J. Biochem.
76
1009-1019
1974
Escherichia coli
brenda
Fitton, J.E.; Shaw, W.V.
Comparison of chloramphenicol acetyltransferase variants in staphylococci. Purification, inhibitor studies and N-terminal sequences
Biochem. J.
177
575-582
1979
Staphylococcus aureus, Staphylococcus epidermidis, Staphylococcus sp.
brenda
Guitard, M.; Daigneault, R.
Purification of Escherichia coli chloramphenicol acetyltransferase by affinity chromatography
Can. J. Biochem.
52
1087-1090
1974
Escherichia coli, Escherichia coli W677/HJR66
brenda
Kleanthous, C.; Shaw, W.V.
Analysis of the mechanism of chloramphenicol acetyltransferase by steady-state kinetics. Evidence for a ternary-complex mechanism
Biochem. J.
223
211-220
1984
Escherichia coli, Escherichia coli J53(R387)
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