Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10-formyltetrahydrofolate + bovine mitochondrial L-methionyl-tRNA
tetrahydrofolate + bovine mitochondrial N-formylmethionyl-tRNA
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-isoleucyl-tRNAfMet
tetrahydrofolate + E. coli N-formylisoleucyl-tRNAfMet
10-formyltetrahydrofolate + E. coli L-methionyl-tRNA1Val(CAU)
tetrahydrofolate + E. coli N-formylisoleucyl-tRNA1Val(CAU)
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-methionyl-tRNAfMet
tetrahydrofolate + E. coli N-formylmethionyl-tRNAfMet
10-formyltetrahydrofolate + E. coli L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
10-formyltetrahydrofolate + E. coli L-methionyl-tRNAmMet
tetrahydrofolate + E. coli N-formylmethionyl-tRNAmMet
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-methionyl-tRNAmMet
tetrahydrofolate + N-formylmethionyl-tRNAmMet
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-valyl-tRNAfMet
tetrahydrofolate + E. coli N-formylvalyl-tRNAfMet
10-formyltetrahydrofolate + E. coli L-valyl-tRNAfMet
tetrahydrofolate + N-formylvalyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + E.coli L-methionyl-tRNAfMet
tetrahydrofolate + E.coli N-formylmethionyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + isoleucyl-tRNAfMet + H2O
tetrahydrofolate + N-formylisoleucyl-tRNAfMet
10-formyltetrahydrofolate + L-isoleucyl-tRNAfMet
tetrahydrofolate + N-formylisoleucyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
10-formyltetrahydrofolate + L-methionyl-tRNAMet
tetrahydrofolate + N-formylmethionyl-tRNAMet
10-formyltetrahydrofolate + L-phenylalanyl-tRNAfMet + H2O
tetrahydrofolate + N-formylphenylalanyl-tRNAfMet
-
mutant tRNA G34A36 is a good substrate
-
-
?
10-formyltetrahydrofolate + methionyl-tRNA1Val(CAU) + H2O
tetrahydrofolate + N-formylmethionyl-tRNA1Val(CAU)
-
mischarged E. coli tRNA1Val(CAU), less efficient than with methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + methionyl-tRNAmMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAmMet
-
E. coli elongator Met-tRNAmMet, less efficient than with methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + phenylalanyl-tRNAfMet + H2O
tetrahydrofolate + N-formylphenylalanyl-tRNAfMet
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
10-formyltetrahydropteroyltriglutamate + L-methionyl-tRNAfMet + H2O
tetrahydropteroyltriglutamate + N-formylmethionyl-tRNAfMet
-
10-formyltetrahydropteroyltriglutamate or 10-formyltetrahydrofolate can act as donor
-
?
additional information
?
-
10-formyltetrahydrofolate + E. coli L-isoleucyl-tRNAfMet
tetrahydrofolate + E. coli N-formylisoleucyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-isoleucyl-tRNAfMet
tetrahydrofolate + E. coli N-formylisoleucyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-methionyl-tRNAfMet
tetrahydrofolate + E. coli N-formylmethionyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-methionyl-tRNAfMet
tetrahydrofolate + E. coli N-formylmethionyl-tRNAfMet
-
-
-
r
10-formyltetrahydrofolate + E. coli L-methionyl-tRNAfMet
tetrahydrofolate + E. coli N-formylmethionyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-valyl-tRNAfMet
tetrahydrofolate + E. coli N-formylvalyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + E. coli L-valyl-tRNAfMet
tetrahydrofolate + E. coli N-formylvalyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + isoleucyl-tRNAfMet + H2O
tetrahydrofolate + N-formylisoleucyl-tRNAfMet
-
mischarged E. coli tRNAfMet
-
-
?
10-formyltetrahydrofolate + isoleucyl-tRNAfMet + H2O
tetrahydrofolate + N-formylisoleucyl-tRNAfMet
-
less efficient than with methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + isoleucyl-tRNAfMet + H2O
tetrahydrofolate + N-formylisoleucyl-tRNAfMet
-
mischarged E. coli tRNAfMet
-
-
?
10-formyltetrahydrofolate + isoleucyl-tRNAfMet + H2O
tetrahydrofolate + N-formylisoleucyl-tRNAfMet
-
250fold reduced catalytic efficiency compared with methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
r
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
Escherichia coli tRNA2fMet
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
r
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
human mt-tRNAMet
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates bovine mitochondrial and E. coli initiator Met-tRNA with equal efficiency, formylates E. coli elongator Met-tRNA at a lower rate
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates bovine mitochondrial and E. coli initiator Met-tRNA with equal efficiency, formylates E. coli elongator Met-tRNA at a lower rate
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
enzyme preferentially recognizes the methionyl moiety of its tRNA substrate, small importance of the tRNA acceptor stem for recognition, E. coli tRNA mutants as substrates
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
broader substrate specificity than that of E. coli enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
broader substrate specificity than that of E. coli enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
recognition mechanism of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
10-formyltetrahydropteroyltriglutamate or 10-formyltetrahydrofolate can also act as donor
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
10-formyltetrahydropteroyltriglutamate or 10-formyltetrahydrofolate can also act as donor
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
determinants for formylation are located in the acceptor stem and D-stem of the initiator tRNA, enzyme binds to the tRNA substrate in an induced fit mechanism, tRNA also undergoes induced structural changes during its binding to enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
role of the linker region between N- and C-terminal domain
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specificity determinants at the end of the acceptor stem of tRNAfMet
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specificity determinants at the end of the acceptor stem of tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
specificity determinants at the end of the acceptor stem of tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
affinity of tRNAfMet for enzyme is improved by aminoacylation
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
affinity of tRNAfMet for enzyme is improved by aminoacylation
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
C-terminal region is very important for enzyme activity: basic amino acids contribute mostly toward the nonspecific binding and orientation of the tRNA 3'-end toward the catalytic site
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
C-terminal region is very important for enzyme activity: basic amino acids contribute mostly toward the nonspecific binding and orientation of the tRNA 3'-end toward the catalytic site
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
1.1 mol 10-L-formyltetrahydrofolate is bound per mol monomeric enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
1.1 mol 10-L-formyltetrahydrofolate is bound per mol monomeric enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
invariant Arg-42 within the 16-amino acid insertion loop, residues 34-49, plays a very important role both in steps of substrate binding and in catalysis, Arg-42 makes functional contacts with the determinants in the acceptor stem of the initiator tRNA
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specificity is restricted to methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specific for methionyl-tRNAfMet, specificity depends exclusively on the nature of tRNA moiety of aminoacylated tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
nucleotide-mutants of tRNAfMet as substrates
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
tRNA substrate binding
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
tRNA substrate binding
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
recognition mechanism of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
recognition mechanism of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
recognition mechanism of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
important role of a 16-amino acid insertion loop in enzyme for tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
important role of a 16-amino acid insertion loop in enzyme for tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
important role of a 16-amino acid insertion loop in enzyme for tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
important role of a 16-amino acid insertion loop in enzyme for tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
keeps in store initiator tRNAfMet for initiation of protein synthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
formyl group provides a positive determinant for IF2, which can select the initiator fMet-tRNA from other tRNAs and a negative determinant, which blocks the binding of EF-Tu to the initiator tRNA
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
enzyme reaction irreversibly commits methionyl-tRNAfMet to initiation of translation in eubacteria
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
key step in the targeting of initiator tRNA towards the translation start machinery in prokaryotes
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
small effect of overproduction of MRF on activity of chloramphenicol acetyltransferase
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
recognition mechanism of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
important role of a 16-amino acid insertion loop in enzyme for tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
recognition mechanism of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
important role of a 16-amino acid insertion loop in enzyme for tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
recognition mechanism of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
important role of a 16-amino acid insertion loop in enzyme for tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
role of the linker region between N- and C-terminal domain
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
specificity determinants at the end of the acceptor stem of tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
C-terminal region is very important for enzyme activity: basic amino acids contribute mostly toward the nonspecific binding and orientation of the tRNA 3'-end toward the catalytic site
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
affinity of tRNAfMet for enzyme is improved by aminoacylation
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
1.1 mol 10-L-formyltetrahydrofolate is bound per mol monomeric enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
affinity of tRNAfMet for enzyme is improved by aminoacylation
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
1.1 mol 10-L-formyltetrahydrofolate is bound per mol monomeric enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
specific for methionyl-tRNAfMet, specificity depends exclusively on the nature of tRNA moiety of aminoacylated tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
role of the linker region between N- and C-terminal domain
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
specificity determinants at the end of the acceptor stem of tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
C-terminal region is very important for enzyme activity: basic amino acids contribute mostly toward the nonspecific binding and orientation of the tRNA 3'-end toward the catalytic site
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from Euglena gracilis or yeast
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
high specificity for initiator tRNAMet, strong positive cooperativity for Met-tRNAfMet and N10-formyltetrahydrofolate
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein synthesis in chloroplasts, other mechanism than in cytoplasm of eukaryotes
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from Euglena gracilis or yeast
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
high specificity for initiator tRNAMet, strong positive cooperativity for Met-tRNAfMet and N10-formyltetrahydrofolate
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein synthesis in chloroplasts, other mechanism than in cytoplasm of eukaryotes
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
Asn-107, His-109 and Asp-145 are catalytic residues, Arg-41 is involved in tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
E. coli tRNAFMet
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates yeast mitochondrial methionyl-tRNAfMet, specific for initiator tRNAs
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
enzyme recognizes nucleotidic features in the acceptor stem of mitochondrial initiator tRNA, recognition mechanism
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
initiation of protein synthesis in mitochondria
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
the dispensable mitochondrial methionyl-tRNAformyltransferase, Fmt1p, is essential for respiratory growth in the absence of Rsm28p
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from wheat germ and leaf
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
component of a protein chain initiating system in chloroplasts
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylation of the methionyl-tRNA-fMet is essential for in vitro binding of imported formylated elongator-type tRNA(Met)
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAMet
tetrahydrofolate + N-formylmethionyl-tRNAMet
-
-
-
-
r
10-formyltetrahydrofolate + L-methionyl-tRNAMet
tetrahydrofolate + N-formylmethionyl-tRNAMet
-
-
-
-
r
10-formyltetrahydrofolate + phenylalanyl-tRNAfMet + H2O
tetrahydrofolate + N-formylphenylalanyl-tRNAfMet
-
mischarged E. coli tRNAfMet, reduced velocity compared to the formylation of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + phenylalanyl-tRNAfMet + H2O
tetrahydrofolate + N-formylphenylalanyl-tRNAfMet
-
7fold less efficient formylation than of methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + phenylalanyl-tRNAfMet + H2O
tetrahydrofolate + N-formylphenylalanyl-tRNAfMet
-
mischarged E. coli tRNAfMet, reduced velocity compared to the formylation of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
-
mischarged E. coli tRNAfMet
-
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
-
less efficiency than with methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
-
mischarged E. coli tRNAfMet
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
-
mischarged E. coli tRNAfMet
-
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
-
130fold less efficient formylation than of methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
-
reduced velocity compared to the formylation of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
-
mischarged E. coli tRNAfMet
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
-
mischarged E. coli tRNAfMet
-
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
-
25fold reduced catalytic efficiency compared with methionyl-tRNAfMet
-
-
?
additional information
?
-
-
no formylation of Val-tRNA1Met
-
-
?
additional information
?
-
-
translational initiation in mitochondria
-
-
?
additional information
?
-
-
translational initiation in mitochondria
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
-
ATP plus L-methionine and either tRNAmMet or tRNAfMet cannot replace methionyl-tRNAfMet
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
-
ATP plus L-methionine and either tRNAmMet or tRNAfMet cannot replace methionyl-tRNAfMet
-
-
?
additional information
?
-
-
no formyl group donor: 5-formyltetrahydrofolate
-
-
?
additional information
?
-
-
mutant tRNAs as poor substrates
-
-
?
additional information
?
-
-
mutant tRNAs as poor substrates
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
-
broad specificity at the level of tRNA binding, formylation of mischarged E. coli tRNAfMet
-
-
?
additional information
?
-
-
no formylation of deacylated heterogenous or deacylated partially purified methionyl-tRNA
-
-
?
additional information
?
-
-
ATP plus L-methionine and either tRNAmMet or tRNAfMet cannot replace methionyl-tRNAfMet
-
-
?
additional information
?
-
-
enzyme structure
-
-
?
additional information
?
-
-
enzyme structure
-
-
?
additional information
?
-
-
enzyme structure
-
-
?
additional information
?
-
enzyme structure
-
-
?
additional information
?
-
-
enzyme structure
-
-
?
additional information
?
-
enzyme structure
-
-
?
additional information
?
-
-
enzyme structure
-
-
?
additional information
?
-
-
no formyl group donor: 5,10-methenyltetrahydrofolate
-
-
?
additional information
?
-
-
no formyl group donor: 5,10-methenyltetrahydrofolate
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
-
ATP plus L-methionine and either tRNAmMet or tRNAfMet cannot replace methionyl-tRNAfMet
-
-
?
additional information
?
-
-
no formylation of deacylated heterogenous or deacylated partially purified methionyl-tRNA
-
-
?
additional information
?
-
-
no formyl group donor: 5,10-methenyltetrahydrofolate
-
-
?
additional information
?
-
-
mutant tRNAs as poor substrates
-
-
?
additional information
?
-
-
enzyme structure
-
-
?
additional information
?
-
-
mutant tRNAs as poor substrates
-
-
?
additional information
?
-
-
enzyme structure
-
-
?
additional information
?
-
-
mutant tRNAs as poor substrates
-
-
?
additional information
?
-
-
enzyme structure
-
-
?
additional information
?
-
-
mutant tRNAs as poor substrates
-
-
?
additional information
?
-
-
enzyme structure
-
-
?
additional information
?
-
-
mutant tRNAs as poor substrates
-
-
?
additional information
?
-
-
enzyme structure
-
-
?
additional information
?
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
enzyme structure
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
-
broad specificity at the level of tRNA binding, formylation of mischarged E. coli tRNAfMet
-
-
?
additional information
?
-
-
no formyl group donor: 5-formyltetrahydrofolate
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
-
no formyl group donor: 5,10-methenyltetrahydrofolate
-
-
?
additional information
?
-
no formylation of methionyl-tRNAmMet
-
-
?
additional information
?
-
enzyme structure
-
-
?
additional information
?
-
-
mutant tRNAs as poor substrates
-
-
?
additional information
?
-
-
formylates mitochondrial methionyl-tRNAfMet from yeast, low-level activity with yeast cytoplasmic and E. coli tRNA
-
-
?
additional information
?
-
-
mitochondrial protein synthesis
-
-
?
additional information
?
-
-
formylates mitochondrial methionyl-tRNAfMet from yeast, low-level activity with yeast cytoplasmic and E. coli tRNA
-
-
?
additional information
?
-
-
mitochondrial protein synthesis
-
-
?
additional information
?
-
-
resistance mutations are identified in the fmt gene encoding the enzyme methionyl-tRNA formyltransferase. In the absence of antibiotic, these resistance mutations confer a fitness cost that is manifested as a reduced growth rate in laboratory medium and in mice
-
-
?
additional information
?
-
-
no formylation of cytoplasmic initiating Met-tRNAi
-
-
?
additional information
?
-
-
no formylation of methionyl-tRNAmMet
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
additional information
?
-
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
keeps in store initiator tRNAfMet for initiation of protein synthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
formyl group provides a positive determinant for IF2, which can select the initiator fMet-tRNA from other tRNAs and a negative determinant, which blocks the binding of EF-Tu to the initiator tRNA
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
enzyme reaction irreversibly commits methionyl-tRNAfMet to initiation of translation in eubacteria
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
key step in the targeting of initiator tRNA towards the translation start machinery in prokaryotes
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
small effect of overproduction of MRF on activity of chloramphenicol acetyltransferase
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein synthesis in chloroplasts, other mechanism than in cytoplasm of eukaryotes
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
involved in initiation of protein synthesis in chloroplasts, other mechanism than in cytoplasm of eukaryotes
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
initiation of protein synthesis in mitochondria
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
the dispensable mitochondrial methionyl-tRNAformyltransferase, Fmt1p, is essential for respiratory growth in the absence of Rsm28p
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
component of a protein chain initiating system in chloroplasts
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
formylation of the methionyl-tRNA-fMet is essential for in vitro binding of imported formylated elongator-type tRNA(Met)
-
-
?
additional information
?
-
-
translational initiation in mitochondria
-
-
?
additional information
?
-
-
translational initiation in mitochondria
-
-
?
additional information
?
-
-
mitochondrial protein synthesis
-
-
?
additional information
?
-
-
mitochondrial protein synthesis
-
-
?
additional information
?
-
-
resistance mutations are identified in the fmt gene encoding the enzyme methionyl-tRNA formyltransferase. In the absence of antibiotic, these resistance mutations confer a fitness cost that is manifested as a reduced growth rate in laboratory medium and in mice
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A172L
site-directed mutagenesis, the mutation causes a 6fold decrease in enzyme activity compared to wild-type, the Vmax/Km of the mutant is about 4fold lower than that of the wild-type enzyme
A172S
site-directed mutagenesis, the mutation does not significantly affect the enzyme activity
A55T
-
no suppressor mutation
A89L
site-directed mutagenesis, the Vmax/Km of the mutant is about 144fold lower than that of the wild-type enzyme
A89S
site-directed mutagenesis, the mutation does not significantly affect the enzyme activity
G178D
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, it compensates for lysine that is attached to the tRNA, G178D, G178K and G178L are progressively weaker suppressors than G178E
G178E
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors
G178K
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors than G178E
G178L
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors than G178E
G41Q
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
R38K
-
mutant enzyme with 2.2fold increased Km, no effect on kcat
R38L
-
mutant enzyme with up to 12fold lower specific activity, 6fold increased Km and 5fold decreased kcat
R42K
-
mutant enzyme with lower activity, 16fold increased Km
R42L
-
single mutant and G41R/R42L double mutant with low activity, R42L: 17fold increased Km and 79fold decreased kcat
R42Q
-
mutant enzyme with lower activity, 16-17fold increased Km
A55T
-
no suppressor mutation
-
G178D
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, it compensates for lysine that is attached to the tRNA, G178D, G178K and G178L are progressively weaker suppressors than G178E
-
G178E
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors
-
G178K
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors than G178E
-
G178L
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors than G178E
-
G41D
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41K
-
suppressor mutation within a 16-amino acid insertion, compensates for the formylation defect of a U35A36/G72G73 mutant initiator tRNA, lacking a critical determinant in the acceptor stem
-
G41L
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41Q
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41R
-
suppressor mutation within a 16-amino acid insertion, compensates for the formylation defect of a U35A36/G72G73 mutant initiator tRNA, lacking a critical determinant in the acceptor stem
-
G41D
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41K
-
suppressor mutation within a 16-amino acid insertion, compensates for the formylation defect of a U35A36/G72G73 mutant initiator tRNA, lacking a critical determinant in the acceptor stem
-
G41L
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41Q
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41R
-
suppressor mutation within a 16-amino acid insertion, compensates for the formylation defect of a U35A36/G72G73 mutant initiator tRNA, lacking a critical determinant in the acceptor stem
-
A55T
-
no suppressor mutation
-
G178D
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, it compensates for lysine that is attached to the tRNA, G178D, G178K and G178L are progressively weaker suppressors than G178E
-
G178E
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors
-
G178K
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors than G178E
-
G178L
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors than G178E
-
G41D
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41K
-
suppressor mutation within a 16-amino acid insertion, compensates for the formylation defect of a U35A36/G72G73 mutant initiator tRNA, lacking a critical determinant in the acceptor stem
-
G41L
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41Q
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41R
-
suppressor mutation within a 16-amino acid insertion, compensates for the formylation defect of a U35A36/G72G73 mutant initiator tRNA, lacking a critical determinant in the acceptor stem
-
D145A
-
mutant enzyme with drastically reduced activity
D145E
-
mutant enzyme with 881fold reduced formylation rate, kinetic parameters
D145N
-
mutant enzyme with 4031fold reduced formylation rate, kinetic parameters
H109A
-
mutant enzyme with 4677fold reduced formylation rate, kinetic parameters
H109K
-
inactive mutant enzyme
H109R
-
mutant enzyme with 7172fold reduced formylation rate, kinetic parameters
K37A
-
mutant enzyme with 3.5fold reduced formylation rate, kinetic parameters
N107A
-
mutant enzyme with 48fold reduced formylation rate, kinetic parameters
R41A
-
mutant enzyme with 470fold reduced formylation rate, kinetic parameters
R41K
-
mutant enzyme with 140fold reduced formylation rate, kinetic parameters
V31A
-
mutant enzyme with 1.7fold reduced formylation rate
A59V
-
the mutation causing substantially decreased enzyme activity is associated with selective vulnerability of the visual pathway and a mild neurological phenotype of Leigh syndrome. The missense mutation destabilizes the protein
R181S
-
the mutation causes severe Leigh syndrome
S125L
naturally occurring mutation, the mutant has a 653fold lower activity compared to the wild-type
S209L
naturally occurring mutation, the mutant has a 36fold lower activity compared to the wild-type
del833
-
inactivated methionyl-tRNA formyltransferase
deltafmt1
-
in combination with mutation of AEP3, a gene encodes for a peripheral mitochondrial inner membrane protein, respiratory defect
G41D
-
mutant enzyme with decreased activity
G41D
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
G41K
-
suppressor mutation within a 16-amino acid insertion, compensates for the formylation defect of a U35A36/G72G73 mutant initiator tRNA, lacking a critical determinant in the acceptor stem
G41K
-
mutant enzyme with decreased activity
G41L
-
mutant enzyme with decreased activity
G41L
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
G41R
-
suppressor mutation within a 16-amino acid insertion, compensates for the formylation defect of a U35A36/G72G73 mutant initiator tRNA, lacking a critical determinant in the acceptor stem
G41R
-
G41R/R42L double mutant with low activity, G41R: decreased activity
additional information
several C-terminal deletion mutants and substitution mutants in the linker region between the C- and N-terminal domain and the C-terminal domain
additional information
-
several C-terminal deletion mutants and substitution mutants in the linker region between the C- and N-terminal domain and the C-terminal domain
additional information
-
several C-terminal deletion mutants and substitution mutants in the linker region between the C- and N-terminal domain and the C-terminal domain
-
additional information
-
several C-terminal deletion mutants and substitution mutants in the linker region between the C- and N-terminal domain and the C-terminal domain
-
additional information
-
mutations of Asp-145 and Arg-41 reduce the affinity for initiator tRNA, mutations of Asn-107 and His-109 affect catalysis but not tRNA binding
additional information
-
insertionally inactivated methionyl-tRNA formyltransferase in mutant CDR1 and mutant CDR2
additional information
-
mutation analysis shows that methionyl-tRNA-formyltransferase Fmt1p, is essential for respiratory growth in the absence of mitochondrial ribosomal protein Rsm28p
additional information
mutation analysis shows that methionyl-tRNA-formyltransferase Fmt1p, is essential for respiratory growth in the absence of mitochondrial ribosomal protein Rsm28p
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Dickerman, H.W.; Steers, E.; Redfield, B.G.; Weissbach, H.
Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization
J. Biol. Chem.
242
1522-1525
1967
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Blanquet, S.; Dessen, P.; Kahn, D.
Properties and specificity of methionyl-tRNAfMet formyltransferase from Escherichia coli
Methods Enzymol.
106
141-152
1984
Escherichia coli, Escherichia coli K12 EM20031(F32)
brenda
Giege, R.; Ebel, J.P.; Clarke, B.F.C.
Formylation of mischarged E. coli tRNA Met f
FEBS Lett.
30
291-295
1973
Escherichia coli, Escherichia coli K12 MO
brenda
Kahn, D.; Fromant, M.; Fayat, G.; Dessen, P.; Blanquet, S.
Methionyl-transfer-RNA transformylase from Escherichia coli. Purification and characterisation
Eur. J. Biochem.
105
489-497
1980
Escherichia coli, Escherichia coli K12 EM20031(F32)
brenda
Guillon, J.M.; Meinnel, T.; Mechulam, Y.; Lazennec, C.; Blanquet, S.; Fayat, G.
Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNA(fMet) formyltransferase
J. Mol. Biol.
224
359-367
1992
Escherichia coli
brenda
Lee, C.P.; Seong, B.L.; RajBhandary, U.L.
Structural and sequence elements important for recognition of Escherichia coli formylmethionine tRNA by methionyl-tRNA transformylase are clustered in the acceptor stem
J. Biol. Chem.
266
18012-18017
1991
Escherichia coli
brenda
Crosti, P.; Gambini, A.; Lucchini, G.; Bianchetti, R.
Eukaryotic N10-formyl-H4folate:methionyl-tRNAf transformylase. Some properties of the Euglena gracilis enzyme
Biochim. Biophys. Acta
477
356-370
1977
Euglena gracilis, Euglena gracilis Z
brenda
Gambini, A.; Crosti, P.; Bianchetti, R.
Inhibitor studies of methionyl-tRNA transformylase of Euglena gracilis
Biochim. Biophys. Acta
613
73-78
1980
Euglena gracilis
brenda
Samuel, C.E.; Rabinowitz, J.C.
Initiation of protein synthesis by folate-sufficient and folate-deficient Streptococcus faecalis R: Partial purification and properties of methionyl-transfer ribonucleic acid synthetase and methionyl-transfer ribonucleic acid formyltransferase
J. Bacteriol.
118
21-31
1974
Escherichia coli, Enterococcus faecalis, Enterococcus faecalis R / ATCC 8043, Escherichia coli A19
brenda
Halbreich, A.; Rabinowitz, M.
Isolation of Saccharomyces cerevisiae mitochondrial formyltetrahydrofolic acid:methionyl-tRNA transformylase and the hybridization of mitochondrial fMet-tRNA with mitochondrial DNA
Proc. Natl. Acad. Sci. USA
68
294-298
1971
Saccharomyces cerevisiae, Saccharomyces cerevisiae D243-2B-R1
brenda
Leis, J.P.; Keller, E.B.
N-formylmethionyl-tRNA of wheat chloroplasts. Its synthesis by a wheat transformylase
Biochemistry
10
889-894
1971
Triticum aestivum
brenda
Schmitt, E.; Panvert, M.; Blanquet, S.; Mechulam, Y.
Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNA
EMBO J.
17
6819-6826
1998
Escherichia coli (P23882)
brenda
Schmitt, E.; Blanquet, S.; Mechulam, Y.
Structure of crystalline Escherichia coli methionyl-tRNAMet formyltransferase: Comparison with glycinamide ribonucleotide formyltransferase
EMBO J.
15
4749-4758
1996
Escherichia coli
brenda
Takeuchi, N.; Ueda, T.; Watanabe, K.
Expression and characterization of bovine mitochondrial methionyl-tRNA transformylase
J. Biochem.
124
1069-1071
1998
Bos taurus
brenda
Takeuchi, N.; Vial, L.; Panvert, M.; Schmitt, E.; Watanabe, K.; Mechulam, Y.; Blanquet, S.
Recognition of tRNAs by methionyl-tRNA transformylase from mammalian mitochondria
J. Biol. Chem.
276
20064-20068
2001
Bos taurus
brenda
Ramesh, V.; Gite, S.; Li, Y.; RajBhandary, U.L.
Suppressor mutations in Escherichia coli methionyl-tRNA formyltransferase: Role of a 16-amino acid insertion module in initiator tRNA recognition
Proc. Natl. Acad. Sci. USA
94
13524-13529
1997
Escherichia coli, Escherichia coli CA274, Escherichia coli DH5-alphaF, Escherichia coli JM109
brenda
Li, Y.; Ramesh, V.; Mangroo, D.; Taneja, C.; RajBhandary, U.L.
Suppressor mutations in Escherichia coli methionyl-tRNA formyltransferase that compensate for the formylation defect of a mutant tRNA aminoacylated with lysine
Biochemistry
39
8039-8046
2000
Escherichia coli, Escherichia coli CA274, Escherichia coli JM109
brenda
Ramesh, V.; Gite, S.; RajBhandary, U.L.
Functional interaction of an arginine conserved in the sixteen amino acid insertion module of Escherichia coli methionyl-tRNA formyltransferase with determinants for formylation in the initiator tRNA
Biochemistry
37
15925-15932
1998
Escherichia coli
brenda
Gite, S.; Li, Y.; Ramesh, V.; RajBhandary, U.L.
Escherichia coli methionyl-tRNA formyltransferase: Role of amino acids conserved in the linker region and in the C-terminal domain on the specific recognition of the initiator tRNA
Biochemistry
39
2218-2226
2000
Escherichia coli (P23882), Escherichia coli, Escherichia coli JM109 (P23882), Escherichia coli XL1-Blue (P23882)
brenda
Vial, L.; Gomez, P.; Panvert, M.; Schmitt, E.; Blanquet, S.; Mechulam, Y.
Mitochondrial methionyl-tRNAfMet formyltransferase from Saccharomyces cerevisiae: Gene disruption and tRNA substrate specificity
Biochemistry
42
932-939
2003
Saccharomyces cerevisiae
brenda
Newton, D.T.; Mangroo, D.
Mapping the active site of the Haemophilus influenzae methionyl-tRNA formyltransferase: Residues important for catalysis and tRNA binding
Biochem. J.
339
63-69
1999
Thermus thermophilus, Haemophilus influenzae, Pseudomonas aeruginosa, Rickettsia prowazekii
-
brenda
Mayer, C.; RajBhandary, U.L.
Conformational change of Escherichia coli initiator methionyl-tRNAfMet upon binding to methionyl-tRNA formyl transferase
Nucleic Acids Res.
30
2844-2850
2002
Escherichia coli (P23882), Escherichia coli
brenda
Mayer, C.; Kohrer, C.; Kenny, E.; Prusko, C.; RajBhandary, U.L.
Anticodon sequence mutants of Escherichia coli initiator tRNA: effects of overproduction of aminoacyl-tRNA synthetases, methionyl-tRNA formyltransferase, and initiation factor 2 on activity in initiation
Biochemistry
42
4787-4799
2003
Escherichia coli
brenda
Charriere, F.; Tan, T.H.; Schneider, A.
Mitochondrial initiation factor 2 of Trypanosoma brucei binds imported formylated elongator-type tRNA(Met)
J. Biol. Chem.
280
15659-15665
2005
Trypanosoma brucei
brenda
Newton, D.T.; Niemkiewicz, M.; Lo, R.Y.; Mangroo, D.
Recognition of the initiator tRNA by the Pseudomonas aeruginosa methionyl-tRNA formyltransferase: importance of the base-base mismatch at the end of the acceptor stem
FEMS Microbiol. Lett.
178
289-298
1999
Escherichia coli, Pseudomonas aeruginosa
brenda
Williams, E.H.; Butler, C.A.; Bonnefoy, N.; Fox, T.D.
Translation initiation in Saccharomyces cerevisiae mitochondria: functionalinteractions among mitochondrial ribosomal protein Rsm28p, initiation factor 2, methionyl-tRNA-formyltransferase and novel protein Rmd9p
Genetics
175
1117-1126
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P32785)
brenda
Nilsson, A.I.; Zorzet, A.; Kanth, A.; Dahlstroem, S.; Berg, O.G.; Andersson, D.I.
Reducing the fitness cost of antibiotic resistance by amplification of initiator tRNA genes
Proc. Natl. Acad. Sci. USA
103
6976-6981
2006
Salmonella enterica
brenda
Caughlan, R.E.; Sriram, S.; Daigle, D.M.; Woods, A.L.; Buco, J.; Peterson, R.L.; Dzink-Fox, J.; Walker, S.; Dean, C.R.
Fmt bypass in Pseudomonas aeruginosa causes induction of MexXY efflux pump expression
Antimicrob. Agents Chemother.
53
5015-5021
2009
Pseudomonas aeruginosa
brenda
Lee, C.; Tibbetts, A.S.; Kramer, G.; Appling, D.R.
Yeast AEP3p is an accessory factor in initiation of mitochondrial translation
J. Biol. Chem.
284
34116-34125
2009
Saccharomyces cerevisiae
brenda
Tucker, E.J.; Hershman, S.G.; Koehrer, C.; Belcher-Timme, C.A.; Patel, J.; Goldberger, O.A.; Christodoulou, J.; Silberstein, J.M.; McKenzie, M.; Ryan, M.T.; Compton, A.G.; Jaffe, J.D.; Carr, S.A.; Calvo, S.E.; RajBhandary, U.L.; Thorburn, D.R.; Mootha, V.K.
Mutations in MTFMT underlie a human disorder of formylation causing impaired mitochondrial translation
Cell Metab.
14
428-434
2011
Homo sapiens
brenda
Pino, P.; Aeby, E.; Foth, B.J.; Sheiner, L.; Soldati, T.; Schneider, A.; Soldati-Favre, D.
Mitochondrial translation in absence of local tRNA aminoacylation and methionyl tRNA Met formylation in Apicomplexa
Mol. Microbiol.
76
706-718
2010
Toxoplasma gondii, Toxoplasma gondii RH
brenda
Lewandowski, T.; Huang, J.; Fan, F.; Rogers, S.; Gentry, D.; Holland, R.; Demarsh, P.; Aubart, K.; Zalacain, M.
Staphylococcus aureus formyl-methionyl transferase mutants demonstrate reduced virulence factor production and pathogenicity
Antimicrob. Agents Chemother.
57
2929-2936
2013
Staphylococcus aureus, Staphylococcus aureus WCUH29
brenda
Sinha, A.; Koehrer, C.; Weber, M.H.; Masuda, I.; Mootha, V.K.; Hou, Y.M.; RajBhandary, U.L.
Biochemical characterization of pathogenic mutations in human mitochondrial methionyl-tRNA formyltransferase
J. Biol. Chem.
289
32729-32741
2014
Escherichia coli (P23882), Escherichia coli, Homo sapiens (Q96DP5), Homo sapiens
brenda
Franco, L.V.R.; Moda, B.S.; Soares, M.A.K.M.; Barros, M.H.
Msc6p is required for mitochondrial translation initiation in the absence of formylated Met-tRNAfMet
FEBS J.
286
1407-1419
2019
Saccharomyces cerevisiae
brenda
La Piana, R.; Weraarpachai, W.; Ospina, L.H.; Tetreault, M.; Majewski, J.; Majewski, J.; Bruce Pike, G.; Decarie, J.C.; Tampieri, D.; Brais, B.; Shoubridge, E.A.
Identification and functional characterization of a novel MTFMT mutation associated with selective vulnerability of the visual pathway and a mild neurological phenotype
Neurogenetics
18
97-103
2017
Homo sapiens
brenda