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Information on EC 2.3.1.28 - chloramphenicol O-acetyltransferase and Organism(s) Escherichia coli and UniProt Accession P62577
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2.3.1.28 chloramphenicol O-acetyltransferaseSpecify your search results
Word Map
- 2.3.1.28
-
5'-flanking
-
cotransfection
-
cis-acting
- tata
-
transactivation
- sp1
-
footprint
-
simian
- thymidine
- hepatoma
- immunodeficiency
- camp
- glucocorticoid
- dnase
- dexamethasone
-
phorbol
-
herpes
-
trans-acting
- simplex
- viruses
- sarcoma
- adenovirus
- c-fos
- nuclease
-
ccaat
-
promoterless
- cytomegalovirus
-
electroporation
-
nf-kappa
-
jurkat
-
run-on
-
dna-protein
-
immediate-early
- e1a
-
5'-deletion
-
gc-rich
- 12-o-tetradecanoylphorbol-13-acetate
-
5\'-upstream
-
camp-responsive
-
supershifted
-
polyhedrosis
-
mobility-shift
-
estrogen-responsive
-
subgenomic
- htlv-i
-
sp1-binding
-
glucocorticoid-responsive
-
basepairs
-
moloney
- analysis
- molecular biology
- medicine
- proviruses
- biotechnology
- synthesis
- pharmacology
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
chloramphenicol acetyltransferase, cat-86, cat i, cat ii, chloramphenicol transacetylase, cat iii, acetyl-coa:chloramphenicol 3-o-acetyltransferase, chloramphenicol o-acetyltransferase, chloramphenicol acetylase, chloramphenicol acetyltransferase b2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyltransferase, chloramphenicol
-
-
-
-
CAT
CAT I
-
-
-
-
CAT III
-
-
-
-
chloramphenicol acetylase
-
-
-
-
chloramphenicol acetyltransferase
chloramphenicol transacetylase
-
-
-
-
CAT
-
-
-
-
chloramphenicol acetyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate
ternary complex mechanism with a rapid equilibrium and essentially random order of addition of substrates
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:chloramphenicol 3-O-acetyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9040-07-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + D-threo-1-p-nitrophenyl-2-bromoacetamido-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
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
identification and prediction of a His-based heme-regulatory motif. Heme interacts with chloroamphenicol acetyltransferase and displays an inhibitory effect on the protein activity
Crystal violet
-
strong, competitive for chloramphenicol, non-competitive for acetyl-CoA
ethyl violet
-
strong, competitive for chloramphenicol, non-competitive for acetyl-CoA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic analysis and profiling using substrate chloramphenicol bound on monolayers on gold chips, recombinant enzyme
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
relative activity: 94.9% (wild-type), 34.6% (fluorinated CAT), 89% (mutant L158I), 51.7% (fluorinated mutant L158I)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme expression is increased at 42°C. At 42°C the enzyme is still soluble and active
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
method development for a sensitive model system for analyzing the rapid delivery of active enzymes into various regions of the brain of Rattus norvegicus with therapeutic bioavailability, intranasal delivery of chloramphenicol acetyltransferase from Escherichia coli, a relatively large enzyme, in its active form into different regions of the brain
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of CATI in the unbound (apo) and CAM-bound forms are refined to 3.2 A and 2.9 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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(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
additional information
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)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ELP (elastin-like polypeptide) fusion tag technique to purify ultra-low levels of chloramphenicol acetyltransferase-ELP fusion protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
valuable tool in studies of eukaryotic gene expression, quantitative aspects of the use of bacterial chloramphenicol acetyltransferase as a reporter system in the yeast Saccharomyces cerevisiae
medicine
-
method development for a sensitive model system for analyzing the rapid delivery of active enzymes into various regions of the brain of Rattus norvegicus with therapeutic bioavailability, intranasal delivery of chloramphenicol acetyltransferase from Escherichia coli, a relatively large enzyme, in its active form into different regions of the brain, overview
molecular biology
pharmacology
-
method development for a sensitive model system for analyzing the rapid delivery of active enzymes into various regions of the brain of Rattus norvegicus with therapeutic bioavailability, intranasal delivery of chloramphenicol acetyltransferase from Escherichia coli, a relatively large enzyme, in its active form into different regions of the brain, overview
molecular biology
-
the chloramphenicol acetyl transferase gene serves as integration target for the eukaryotic mariner transposon Mos1 regardless of the location (chromosome or plasmid), as tested with in vitro and bacterial transposition assays
molecular biology
-
single-chain variable fragment (scFv) phages are selected with affinity for CAT. Surface plasmon resonance analyses shows that the tested scFv phages have an affinity for CAT with a dissociation constant (Kd) around 1 microM. The selected scFv phages can be used as capture elements in a highly sensitive sandwich ELISA to detect CAT concentration as low as 0.1 ng/ml or 4 pM
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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.
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
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
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
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
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
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)
Van der Schueren, J.; Robben, J.; Volckaert, G.
Misfolding of chloramphenicol acetyltransferase due to carboxy-terminal truncation can be corrected by second-site mutations
Protein Eng.
11
1211-1217
1998
Escherichia coli
Kim, S.J.; Jeon, H.Y.; Kim, H.B.
Chloramphenicol acetyltransferase expression of Escherichia coli is increased at 42 DegC
Biotechnol. Tech.
11
435-438
1997
Escherichia coli
-
Zhou, M.; Lu, M.L.; Qiu, W.; Campbell, R.L.; Nahoum, V.; Lapointe, J.; Roy, P.H.; Lin, S.X.
Crystallization and preliminary X-ray diffraction analysis of the chloramphenicol acetyltransferase from Tn2424
Acta Crystallogr. Sect. D
57
281-283
2001
Escherichia coli
Day, P.J.; Murray, I.A.; Shaw, W.V.
Properties of hybrid active sites in oligomeric proteins: kinetic and ligand binding studies with chloramphenicol acetyltransferase trimers
Biochemistry
34
6416-6422
1995
Escherichia coli
Van der Schueren, J.; Robben, J.; Goossens, K.; Heremans, K.; Volckaert, G.
Identification of local carboxy-terminal hydrophobic interactions essential for folding or stability of chloramphenicol acetyltransferase
J. Mol. Biol.
256
878-888
1996
Escherichia coli
Alipour, H.; Eriksson, P.; Norbeck, J.; Blomberg, A.
Quantitative aspects of the use of bacterial chloramphenicol acetyltransferase as a reporter system in the yeast Saccharomyces cerevisiae
Anal. Biochem.
270
153-158
1999
Escherichia coli
Qiu, W.; Shi, R.; Lu, M.L.; Zhou, M.; Roy, P.H.; Lapointe, J.; Lin, S.X.
Crystal structure of chloramphenicol acetyltransferase B2 encoded by the multiresistance transposon Tn2424
Proteins
57
858-861
2004
Escherichia coli
Christensen, T.; Trabbic-Carlson, K.; Liu, W.; Chilkoti, A.
Purification of recombinant proteins from Escherichia coli at low expression levels by inverse transition cycling
Anal. Biochem.
360
166-168
2007
Escherichia coli
Panchenko, T.; Zhu, W.W.; Montclare, J.K.
Influence of global fluorination on chloramphenicol acetyltransferase activity and stability
Biotechnol. Bioeng.
94
921-930
2006
Escherichia coli
Voloshchuk, N.; Lee, M.X.; Zhu, W.W.; Tanrikulu, I.C.; Montclare, J.K.
Fluorinated chloramphenicol acetyltransferase thermostability and activity profile: Improved thermostability by a single-isoleucine mutant
Bioorg. Med. Chem. Lett.
17
5907-5911
2007
Escherichia coli
Eom, H.J.; Park, J.M.; Seo, M.J.; Kim, M.D.; Han, N.S.
2 Monitoring of Leuconostoc mesenteroides DRC starter in fermented vegetable by random integration of chloramphenicol acetyltransferase gene
J. Ind. Microbiol. Biotechnol.
35
953-959
2008
Escherichia coli, Staphylococcus sp.
Van Dorst, B.; Mehta, J.; Rouah-Martin, E.; Backeljau, J.; De Coen, W.; Eeckhout, D.; De Jaeger, G.; Blust, R.; Robbens, J.
Selection of scFv phages specific for chloramphenicol acetyl transferase (CAT), as alternatives for antibodies in CAT detection assays
J. Appl. Toxicol.
32
783-789
2012
Escherichia coli
Biswas, T.; Houghton, J.L.; Garneau-Tsodikova, S.; Tsodikov, O.V.
The structural basis for substrate versatility of chloramphenicol acetyltransferase CATI
Protein Sci.
21
520-530
2012
Escherichia coli (P62577)
Choi, I.; Kim, D.E.; Ahn, J.H.; Yeo, W.S.
On-chip enzymatic assay for chloramphenicol acetyltransferase using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
Colloids Surf. B Biointerfaces
136
465-469
2015
Escherichia coli
Appu, A.P.; Arun, P.; Krishnan, J.K.; Moffett, J.R.; Namboodiri, A.M.
Rapid intranasal delivery of chloramphenicol acetyltransferase in the active form to different brain regions as a model for enzyme therapy in the CNS
J. Neurosci. Methods
259
129-134
2016
Escherichia coli
Brewitz, H.H.; Goradia, N.; Schubert, E.; Galler, K.; Kuehl, T.; Syllwasschy, B.; Popp, J.; Neugebauer, U.; Hagelueken, G.; Schiemann, O.; Ohlenschlaeger, O.; Imhof, D.
Heme interacts with histidine- and tyrosine-based protein motifs and inhibits enzymatic activity of chloramphenicol acetyltransferase from Escherichia coli
Biochim. Biophys. Acta
1860
1343-1353
2016
Escherichia coli (P62577), Escherichia coli
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