2.3.2.12: peptidyltransferase
This is an abbreviated version!
For detailed information about peptidyltransferase, go to the full flat file.
Word Map on EC 2.3.2.12
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2.3.2.12
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rrnas
-
puromycin
-
aminoacyl-trnas
-
exit
-
tunnel
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p-site
-
chloramphenicol
-
macrolide
-
decoding
-
aminoacylated
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erythromycin
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stall
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trnaphe
-
haloarcula
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peptide-bond
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protuberance
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oxazolidinones
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lincosamide
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transpeptidation
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penicillin-binding
-
polyu
-
cryo-electron
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ribozyme
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streptogramins
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carbapenems
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anticodon
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linezolid
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ribosome-bound
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marismortui
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pleuromutilins
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clarithromycin
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polyphenylalanine
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polyu-directed
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ketolide
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virginiamycin
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lincomycin
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fmet-trna
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polyphe
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blasticidin
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aa-trnas
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tylosin
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phe-trna
-
clindamycin
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pseudouridine
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medicine
-
spiramycin
- 2.3.2.12
- rrnas
- puromycin
- aminoacyl-trnas
-
exit
-
tunnel
-
p-site
- chloramphenicol
-
macrolide
-
decoding
-
aminoacylated
- erythromycin
-
stall
- trnaphe
-
haloarcula
-
peptide-bond
-
protuberance
-
oxazolidinones
-
lincosamide
-
transpeptidation
-
penicillin-binding
- polyu
-
cryo-electron
-
ribozyme
-
streptogramins
- carbapenems
-
anticodon
- linezolid
-
ribosome-bound
- marismortui
-
pleuromutilins
- clarithromycin
-
polyphenylalanine
-
polyu-directed
-
ketolide
-
virginiamycin
- lincomycin
-
fmet-trna
-
polyphe
-
blasticidin
-
aa-trnas
- tylosin
- phe-trna
- clindamycin
- pseudouridine
- medicine
- spiramycin
Reaction
Synonyms
ArfB, L,D-transpeptidase, L,D-transpeptidase 2, LD-transpeptidase, LDT, LdtD, Ldtfm, LdtMt2, LdtMt5, MSMEI_5283, peptidoglycan transpeptidase, peptidyl transferase, peptidyl transferase center, peptidyltransferase centre, PT, PTase, PTC, PTH, ribosomal peptidyl transferase, ribosomal peptidyltransferase, ribosomal protein L27, transpeptidase
ECTree
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Metals Ions
Metals Ions on EC 2.3.2.12 - peptidyltransferase
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Mg2+
Mg2+
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the velocity of the reaction measured at limiting concentrations of Met-tRNA and saturating puromycin increases with Mg2+ concentration up to about 100 mM
Mg2+
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the ribosomal peptidyl transferase center is supported by a framework of magnesium microclusters. Common features of Mg2+-microclusters include two paired Mg2+ ions that are chelated by a common bridging phosphate group in the form Mg2+(a)-(O1P-PO2P)-Mg2+(b). This bridging phosphate is part of a 10-membered chelation ring in the form Mg2+(a)-(OP-P-O5'-C5'-C4'-C3'-O3'-P-OP)-Mg2+(a). The two phosphate groups of this 10-membered ring are contributed by adjacent residues along the RNA backbone. Both Mg2+ ions are octahedrally coordinated, but are substantially dehydrated by interactions with additional RNA phosphate groups. The Mg2+-microclusters in the large subunit appear to be highly conserved over evolution