2.3.1.28: chloramphenicol O-acetyltransferase
This is an abbreviated version!
For detailed information about chloramphenicol O-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.28
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2.3.1.28
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5'-flanking
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cotransfection
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cis-acting
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tata
-
transactivation
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sp1
-
footprint
-
simian
-
thymidine
-
hepatoma
-
immunodeficiency
-
camp
-
glucocorticoid
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dnase
-
dexamethasone
-
phorbol
-
herpes
-
trans-acting
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simplex
-
viruses
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sarcoma
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adenovirus
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c-fos
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nuclease
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ccaat
-
promoterless
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cytomegalovirus
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electroporation
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nf-kappa
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jurkat
-
run-on
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dna-protein
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immediate-early
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e1a
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5'-deletion
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gc-rich
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12-o-tetradecanoylphorbol-13-acetate
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5\'-upstream
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camp-responsive
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supershifted
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polyhedrosis
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mobility-shift
-
estrogen-responsive
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subgenomic
-
htlv-i
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sp1-binding
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glucocorticoid-responsive
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basepairs
-
moloney
-
analysis
-
molecular biology
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medicine
-
proviruses
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biotechnology
-
synthesis
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pharmacology
- 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
Reaction
Synonyms
acetyltransferase, chloramphenicol, CAP acetyltransferase, CAT, CAT I, CAT II, CAT III, cat-86, CATC, CATI, chloramphenicol acetylase, chloramphenicol acetyltransferase, chloramphenicol acetyltransferase B2, chloramphenicol transacetylase, Pacat, Tn9 ca
ECTree
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Crystallization
Crystallization on EC 2.3.1.28 - chloramphenicol O-acetyltransferase
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crystal structure of CATI in the unbound (apo) and CAM-bound forms are refined to 3.2 A and 2.9 A resolution, respectively
homology modeling of structure. The binding pocket consists of Tyr20, Phe27, Tyr50, Thr88, Ile89, Phe90, Phe97, Ser140, Leu141, Ser142, Ile143, Ile144, Pro145, Trp146, Phe152, Leu154, Ile166, Ile167, Thr168, His189, Asp193, Gly194, and Tyr195, where His189 and Asp193 are the catalytic sites
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