Cloned (Comment) | Organism |
---|---|
gene encoding MTF is cloned and sequenced, expression of wild-type and mutant enzymes in Escherichia coli | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
crystal structure of enzyme complexed with formylmethionyl-tRNAfMet | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
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 | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | values for several mutant enzymes in the linker region and C-terminal domain | Escherichia coli | |
0.0005 | - |
E. coli L-methionyl-tRNAfMet | - |
Escherichia coli | |
0.0037 | - |
L-methionyl-tRNAfMet | MTFDeltaC20 | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | Escherichia coli | involved in initiation of protein biosynthesis | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P23882 | - |
- |
Escherichia coli JM109 | P23882 | - |
- |
Escherichia coli XL1-Blue | P23882 | - |
- |
Purification (Comment) | Organism |
---|---|
purification of His-tagged wild-type and C-terminal deletion mutant recombinant enzymes, expressed in Escherichia coli | Escherichia coli |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
10-formyltetrahydrofolate + E. coli L-methionyl-tRNAfMet | - |
Escherichia coli | tetrahydrofolate + E. coli N-formylmethionyl-tRNAfMet | - |
r | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet | - |
Escherichia coli | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
r | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | role of the linker region between N- and C-terminal domain | Escherichia coli | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | specificity determinants at the end of the acceptor stem of tRNAfMet | Escherichia coli | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | 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 | Escherichia coli | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | specificity is restricted to methionyl-tRNAfMet | Escherichia coli | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | recognition mechanism of methionyl-tRNAfMet | Escherichia coli | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | important role of a 16-amino acid insertion loop in enzyme for tRNA recognition | Escherichia coli | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | involved in initiation of protein biosynthesis | Escherichia coli | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | role of the linker region between N- and C-terminal domain | Escherichia coli JM109 | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | specificity determinants at the end of the acceptor stem of tRNAfMet | Escherichia coli JM109 | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | 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 | Escherichia coli JM109 | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | role of the linker region between N- and C-terminal domain | Escherichia coli XL1-Blue | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | specificity determinants at the end of the acceptor stem of tRNAfMet | Escherichia coli XL1-Blue | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O | 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 | Escherichia coli XL1-Blue | tetrahydrofolate + N-formylmethionyl-tRNAfMet | - |
? | |
additional information | no formylation of methionyl-tRNAmMet | Escherichia coli | ? | - |
? | |
additional information | enzyme structure | Escherichia coli | ? | - |
? | |
additional information | no formylation of methionyl-tRNAmMet | Escherichia coli JM109 | ? | - |
? | |
additional information | enzyme structure | Escherichia coli JM109 | ? | - |
? | |
additional information | no formylation of methionyl-tRNAmMet | Escherichia coli XL1-Blue | ? | - |
? | |
additional information | enzyme structure | Escherichia coli XL1-Blue | ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | values for several mutant enzymes in the linker region and C-terminal domain | Escherichia coli | |
0.2 | - |
L-methionyl-tRNAfMet | MTFDeltaC20 | Escherichia coli | |
37.3 | - |
L-methionyl-tRNAfMet | wild-type enzyme | Escherichia coli |