Information on EC 2.1.2.9 - methionyl-tRNA formyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.1.2.9
-
RECOMMENDED NAME
GeneOntology No.
methionyl-tRNA formyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
10-formyltetrahydrofolate + L-methionyl-tRNAfMet = tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
formyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
One carbon pool by folate
-
SYSTEMATIC NAME
IUBMB Comments
10-formyltetrahydrofolate:L-methionyl-tRNA N-formyltransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
FMT
-
-
-
-
formylmethionyl-transfer ribonucleic synthetase
-
-
-
-
methionyl ribonucleic formyltransferase
-
-
-
-
methionyl-transfer ribonucleic transformylase
-
-
-
-
methionyl-transfer RNA transformylase
-
-
-
-
methionyl-tRNA formyltransferase
-
-
methionyl-tRNA formyltransferase
-
-
methionyl-tRNA formyltransferase
-
-
methionyl-tRNA formyltransferase
-
-
-
methionyl-tRNA Met formyltransferase
-
-
-
-
methionyl-tRNA transformylase
-
-
-
-
methionyl-tRNA-Formyltransferase
-
-
methyltransferase, methionyl-transfer ribonucleate
-
-
-
-
mitochondrial methionyl-tRNA formyltransferase
-
-
MTF
-
-
-
-
MTFMT
-
-
N10-formyltetrahydrofolic-methionyl-transfer ribonucleic transformylase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9015-76-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Enterococcus faecalis R
strain R
-
-
Manually annotated by BRENDA team
strain A19
-
-
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
strain CA274; strain DH5AlphaF'; strain JM109
-
-
Manually annotated by BRENDA team
strain CA274; strain JM109; strains DH5Alpha, Novablue(DE3) pLysS
-
-
Manually annotated by BRENDA team
strain JM109; strain XL1-Blue
Uniprot
Manually annotated by BRENDA team
strain K12 EM20031(F32)
-
-
Manually annotated by BRENDA team
strain K12 MO (lot 15-290)
-
-
Manually annotated by BRENDA team
Escherichia coli A19
strain A19
-
-
Manually annotated by BRENDA team
Escherichia coli CA274
strain CA274
-
-
Manually annotated by BRENDA team
Escherichia coli DH5AlphaF
strain DH5AlphaF'
-
-
Manually annotated by BRENDA team
Escherichia coli JM109
strain JM109
-
-
Manually annotated by BRENDA team
Escherichia coli JM109
strain JM109
Uniprot
Manually annotated by BRENDA team
Escherichia coli K12 EM20031(F32)
strain K12 EM20031(F32)
-
-
Manually annotated by BRENDA team
Escherichia coli K12 MO
strain K12 MO (lot 15-290)
-
-
Manually annotated by BRENDA team
Escherichia coli XL1-Blue
strain XL1-Blue
Uniprot
Manually annotated by BRENDA team
strain Z
-
-
Manually annotated by BRENDA team
Euglena gracilis Z
strain Z
-
-
Manually annotated by BRENDA team
strain D243-2B-R1
-
-
Manually annotated by BRENDA team
strains CMY214, W303, YPALS, DBY2057
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae D243-2B-R1
strain D243-2B-R1
-
-
Manually annotated by BRENDA team
possesses a single gene coding for each FMT and peptide deformylase, PDF, respectively
-
-
Manually annotated by BRENDA team
possesses a single gene coding for each FMT and peptide deformylase, PDF, respectively
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
slow growth of cells when methionyl-tRNA formyltransferase inactive, when enzyme inactive higher transcript titer of MexXY efflux pump
malfunction
-
despite deletion of gene for methionyl-tRNA still initiation of mitochondrial protein syntesis by nonformylatet Met-tRNA
malfunction
-
heterozygous mutations in MTFMT occur in two unrelated children presenting with Leigh syndrome and combined OXPHOS deficiency. The patient fibroblasts have dramatically reduced fMet-tRNAMet levels and an abnormal formylation profile of mitochondrially translated COX1, and patient fibroblasts exhibit severe defects in mitochondrial translation that can be rescued by exogenous expression of MTFMT. Mitochondrial tRNAMet pools are abnormal in patient fibroblasts, phenotypes, overview
metabolism
-
formylmethionine-independent initiation of translation in apicomplexans, the requirement for an initiation by a specialized tRNA charged with formylmethionine is bypassed in the mitochondrion of these parasites, the formylated methionine used during initiation is deformylated on the nascent peptide by a peptide deformylase
physiological function
-
influence on protein synthesis in mitochondria and chloroplasts by producing a formylated initiator methionyl-tRNA
physiological function
-
MTFMT is critical for efficient human mitochondrial translation
metabolism
-
formylmethionine-independent initiation of translation in apicomplexans, the requirement for an initiation by a specialized tRNA charged with formylmethionine is bypassed in the mitochondrion of these parasites, the formylated methionine used during initiation is deformylated on the nascent peptide by a peptide deformylase
-
additional information
-
in Toxoplasma gondii the absence of mitochondrial tRNA genes is compensated for by the import of cytosolic eukaryotic tRNAs. Although all compartments require a complete set of charged tRNAs, the apicomplexan nuclear genomes do not hold sufficient aminoacyl-tRNA synthetase genes to be targeted individually to each compartment. The absence of tRNAMet formyltransferase and peptide deformylase implies that the requirement for a specialized formylmethionyl-tRNAMet for translation initiation is bypassed in the mitochondrion
additional information
-
in Toxoplasma gondii the absence of mitochondrial tRNA genes is compensated for by the import of cytosolic eukaryotic tRNAs. Although all compartments require a complete set of charged tRNAs, the apicomplexan nuclear genomes do not hold sufficient aminoacyl-tRNA synthetase genes to be targeted individually to each compartment. The absence of tRNAMet formyltransferase and peptide deformylase implies that the requirement for a specialized formylmethionyl-tRNAMet for translation initiation is bypassed in the mitochondrion
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
10-formyltetrahydrofolate + isoleucyl-tRNAfMet + H2O
tetrahydrofolate + N-formylisoleucyl-tRNAfMet
show the reaction diagram
-
mischarged E. coli tRNAfMet
-
-
?
10-formyltetrahydrofolate + isoleucyl-tRNAfMet + H2O
tetrahydrofolate + N-formylisoleucyl-tRNAfMet
show the reaction diagram
-
mischarged E. coli tRNAfMet
-
-
?
10-formyltetrahydrofolate + isoleucyl-tRNAfMet + H2O
tetrahydrofolate + N-formylisoleucyl-tRNAfMet
show the reaction diagram
-
250fold reduced catalytic efficiency compared with methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + isoleucyl-tRNAfMet + H2O
tetrahydrofolate + N-formylisoleucyl-tRNAfMet
show the reaction diagram
-
less efficient than with methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P32785, -
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates yeast mitochondrial methionyl-tRNAfMet, specific for initiator tRNAs
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from Euglena gracilis or yeast
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
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
show the reaction diagram
P23882
role of the linker region between N- and C-terminal domain
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
10-formyltetrahydropteroyltriglutamate or 10-formyltetrahydrofolate can also act as donor
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from wheat germ and leaf
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
specificity determinants at the end of the acceptor stem of tRNAfMet
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
specificity determinants at the end of the acceptor stem of tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P23882
specificity determinants at the end of the acceptor stem of tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
affinity of tRNAfMet for enzyme is improved by aminoacylation
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
affinity of tRNAfMet for enzyme is improved by aminoacylation
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P23882
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
show the reaction diagram
-
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
show the reaction diagram
-
1.1 mol 10-L-formyltetrahydrofolate is bound per mol monomeric enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
1.1 mol 10-L-formyltetrahydrofolate is bound per mol monomeric enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from E. coli
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
formylates methionyl-tRNAfMet from E. coli
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
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
show the reaction diagram
-
specificity is restricted to methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P23882
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
specificity is restricted to methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
broader substrate specificity than that of E. coli enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
broader substrate specificity than that of E. coli enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
nucleotide-mutants of tRNAfMet as substrates
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
enzyme recognizes nucleotidic features in the acceptor stem of mitochondrial initiator tRNA, recognition mechanism
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
high specificity for initiator tRNAMet, strong positive cooperativity for Met-tRNAfMet and N10-formyltetrahydrofolate
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
tRNA substrate binding
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
tRNA substrate binding
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
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
show the reaction diagram
P23882
recognition mechanism of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
recognition mechanism of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P23882
recognition mechanism of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
recognition mechanism of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
important role of a 16-amino acid insertion loop in enzyme for tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
important role of a 16-amino acid insertion loop in enzyme for tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P23882
important role of a 16-amino acid insertion loop in enzyme for tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
important role of a 16-amino acid insertion loop in enzyme for tRNA recognition
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
keeps in store initiator tRNAfMet for initiation of protein synthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P23882
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
component of a protein chain initiating system in chloroplasts
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
initiation of protein synthesis in mitochondria
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P23882
enzyme reaction irreversibly commits methionyl-tRNAfMet to initiation of translation in eubacteria
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
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
show the reaction diagram
-
formylation of the methionyl-tRNA-fMet is essential for in vitro binding of imported formylated elongator-type tRNA(Met)
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
small effect of overproduction of MRF on activity of chloramphenicol acetyltransferase
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
E. coli tRNAFMet
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P32785, -
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
show the reaction diagram
Escherichia coli DH5AlphaF
-
recognition mechanism of methionyl-tRNAfMet, important role of a 16-amino acid insertion loop in enzyme for tRNA recognition, involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Euglena gracilis Z
-
formylates methionyl-tRNAfMet from Euglena gracilis or yeast, formylates methionyl-tRNAfMet from E. coli, high specificity for initiator tRNAMet, strong positive cooperativity for Met-tRNAfMet and N10-formyltetrahydrofolate
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Euglena gracilis Z
-
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
show the reaction diagram
Escherichia coli K12 MO
-
formylates methionyl-tRNAfMet from E. coli, specific for methionyl-tRNAfMet, specificity depends exclusively on the nature of tRNA moiety of aminoacylated tRNAfMet, involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli JM109
-
recognition mechanism of methionyl-tRNAfMet, important role of a 16-amino acid insertion loop in enzyme for tRNA recognition, involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli JM109
-
specificity is restricted to methionyl-tRNAfMet, involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli A19
-
specificity is restricted to methionyl-tRNAfMet, involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Enterococcus faecalis R
-
10-formyltetrahydropteroyltriglutamate or 10-formyltetrahydrofolate can also act as donor, specificity is restricted to methionyl-tRNAfMet, involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli K12 EM20031(F32)
-
affinity of tRNAfMet for enzyme is improved by aminoacylation, 1.1 mol 10-L-formyltetrahydrofolate is bound per mol monomeric enzyme, formylates methionyl-tRNAfMet from E. coli
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli K12 EM20031(F32)
-
affinity of tRNAfMet for enzyme is improved by aminoacylation, 1.1 mol 10-L-formyltetrahydrofolate is bound per mol monomeric enzyme
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli CA274
-
recognition mechanism of methionyl-tRNAfMet, important role of a 16-amino acid insertion loop in enzyme for tRNA recognition, involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli CA274
-
specificity is restricted to methionyl-tRNAfMet, involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-phenylalanyl-tRNAfMet + H2O
tetrahydrofolate + N-formylphenylalanyl-tRNAfMet
show the reaction diagram
-
mutant tRNA G34A36 is a good substrate
-
-
?
10-formyltetrahydrofolate + methionyl-tRNA1Val(CAU) + H2O
tetrahydrofolate + N-formylmethionyl-tRNA1Val(CAU)
show the reaction diagram
-
mischarged E. coli tRNA1Val(CAU), less efficient than with methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + methionyl-tRNAmMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAmMet
show the reaction diagram
-
E. coli elongator Met-tRNAmMet, less efficient than with methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + phenylalanyl-tRNAfMet + H2O
tetrahydrofolate + N-formylphenylalanyl-tRNAfMet
show the reaction diagram
-
mischarged E. coli tRNAfMet, reduced velocity compared to the formylation of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + phenylalanyl-tRNAfMet + H2O
tetrahydrofolate + N-formylphenylalanyl-tRNAfMet
show the reaction diagram
-
7fold less efficient formylation than of methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + phenylalanyl-tRNAfMet + H2O
tetrahydrofolate + N-formylphenylalanyl-tRNAfMet
show the reaction diagram
Escherichia coli K12 MO
-
mischarged E. coli tRNAfMet, reduced velocity compared to the formylation of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
show the reaction diagram
-
mischarged E. coli tRNAfMet
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
show the reaction diagram
-
mischarged E. coli tRNAfMet
-
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
show the reaction diagram
-
mischarged E. coli tRNAfMet
-
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
show the reaction diagram
-
mischarged E. coli tRNAfMet
-
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
show the reaction diagram
-
25fold reduced catalytic efficiency compared with methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
show the reaction diagram
-
less efficiency than with methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
show the reaction diagram
-
130fold less efficient formylation than of methionyl-tRNAfMet
-
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
show the reaction diagram
-
reduced velocity compared to the formylation of methionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + valyl-tRNAfMet + H2O
tetrahydrofolate + N-formylvalyl-tRNAfMet
show the reaction diagram
Escherichia coli K12 MO
-
mischarged E. coli tRNAfMet
-
?
10-formyltetrahydropteroyltriglutamate + L-methionyl-tRNAfMet + H2O
tetrahydropteroyltriglutamate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
10-formyltetrahydropteroyltriglutamate or 10-formyltetrahydrofolate can act as donor
-
?
additional information
?
-
-
no formylation of cytoplasmic initiating Met-tRNAi
-
-
-
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
?
-
P23882
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 Val-tRNA1Met
-
-
-
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
?
-
-
formylates mitochondrial methionyl-tRNAfMet from yeast, low-level activity with yeast cytoplasmic and E. coli tRNA
-
-
-
additional information
?
-
-
enzyme structure
-
-
-
additional information
?
-
P23882
enzyme structure
-
-
-
additional information
?
-
-
enzyme structure
-
-
-
additional information
?
-
-
no formyl group donor: 5,10-methenyltetrahydrofolate
-
-
-
additional information
?
-
-
translational initiation in mitochondria
-
-
-
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
?
-
Escherichia coli DH5AlphaF
-
mutant tRNAs as poor substrates, enzyme structure
-
-
-
additional information
?
-
Escherichia coli JM109
-
mutant tRNAs as poor substrates, enzyme structure
-
-
-
additional information
?
-
Escherichia coli JM109
-
mutant tRNAs as poor substrates, enzyme structure
-
-
-
additional information
?
-
Escherichia coli A19
-
no formylation of methionyl-tRNAmMet, ATP plus L-methionine and either tRNAmMet or tRNAfMet cannot replace methionyl-tRNAfMet
-
-
-
additional information
?
-
Enterococcus faecalis R
-
no formylation of methionyl-tRNAmMet, ATP plus L-methionine and either tRNAmMet or tRNAfMet cannot replace methionyl-tRNAfMet
-
-
-
additional information
?
-
Escherichia coli K12 EM20031(F32)
-
no formylation of methionyl-tRNAmMet, broad specificity at the level of tRNA binding, formylation of mischarged E. coli tRNAfMet
-
-
-
additional information
?
-
Escherichia coli K12 EM20031(F32)
-
no formyl group donor: 5-formyltetrahydrofolate, no formylation of methionyl-tRNAmMet, no formyl group donor: 5,10-methenyltetrahydrofolate
-
-
-
additional information
?
-
Saccharomyces cerevisiae D243-2B-R1
-
formylates mitochondrial methionyl-tRNAfMet from yeast, low-level activity with yeast cytoplasmic and E. coli tRNA, mitochondrial protein synthesis
-
-
-
additional information
?
-
Escherichia coli CA274
-
mutant tRNAs as poor substrates, enzyme structure
-
-
-
additional information
?
-
Escherichia coli CA274
-
mutant tRNAs as poor substrates, enzyme structure
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
-
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
keeps in store initiator tRNAfMet for initiation of protein synthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P23882
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
component of a protein chain initiating system in chloroplasts
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
initiation of protein synthesis in mitochondria
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P23882
enzyme reaction irreversibly commits methionyl-tRNAfMet to initiation of translation in eubacteria
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
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
show the reaction diagram
-
formylation of the methionyl-tRNA-fMet is essential for in vitro binding of imported formylated elongator-type tRNA(Met)
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
-
small effect of overproduction of MRF on activity of chloramphenicol acetyltransferase
-
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
P32785, -
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
show the reaction diagram
Escherichia coli DH5AlphaF
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Euglena gracilis Z
-
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
show the reaction diagram
Escherichia coli K12 MO
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli JM109
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli JM109
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli A19, Enterococcus faecalis R
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli CA274
-
involved in initiation of protein biosynthesis
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O
tetrahydrofolate + N-formylmethionyl-tRNAfMet
show the reaction diagram
Escherichia coli CA274
-
involved in initiation of protein biosynthesis
-
?
additional information
?
-
-
translational initiation in mitochondria
-
-
-
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
?
-
Saccharomyces cerevisiae D243-2B-R1
-
mitochondrial protein synthesis
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10-formyltetrahydrofolate
-
1.1 mol 10-L-formyltetrahydrofolate is bound per mol monomeric enzyme
10-formyltetrahydrofolate
-
-
10-formyltetrahydrofolate
-
-
tetrahydrofolate
-
-
tetrahydrofolate
-
-
tetrahydrofolate
-
-
10-formyltetrahydrofolate
-
-
additional information
-
no cofactors: ATP, GTP; no cofactors: ribonucleotide mono- or triphosphates
-
additional information
-
no cofactors: ribonucleotide mono- or triphosphates
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
can partially replace Mg2+
K+
-
can partially replace Mg2+
K+
-
activity is maximum in presence of 7 mM MgCl2 and 150 mM KCl
K+
-
requirement, maximum activity at 10 mM Mg2+ and 150 mM KCl
K+
-
partial requirement, in presence of 8 mM Mg2+ optimum concentration is 20 mM
K+
-
activates, maximum activity at 5 mM Mg2+ and 20 mM KCl
Mg2+
-
activity is maximum in presence of 7 mM MgCl2 and 150 mM KCl
Mg2+
-
maximum activity at 10 mM Mg2+ and 150 mM KCl; requirement
Mg2+
-
partial requirement, optimum concentration is 8 mM, 3fold increased activity
Mg2+
-
optimal concentration: 30 mM; requirement
Mg2+
-
optimal concentration: 30 mM; requirement
Mg2+
-
maximum activity at 5 mM Mg2+ and 20 mM KCl; requirement
Na+
-
activates, can partially replace Mg2+
Na+
-
activates, can partially replace Mg2+
Na+
-
activates, can replace K+
NH4+
-
activates, can partially replace Mg2+
NH4+
-
activates, can partially replace Mg2+
NH4+
-
activates, can replace K+
spermine
-
activates, can partially replace Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10-Formylaminopterin
-
0.01 mM: 38% inhibition, 0.1 mM: 62% inhibition, competitive
10-formylpteroylglutamic acid
-
0.1 mM: 31% inhibition, 1 mM: 52% inhibition, competitive
5,10-methylenetetrahydrofolate
-
-
5-formyltetrahydrofolate
-
competitive inhibition
5-methyltetrahydrofolate
-
most effective, non-competitive inhibitor
aminopterin
-
1 mM: 26% inhibition, competitive inhibition
reduced aminopterin
-
1 mM, 34% inhibition, competitive inhibition
tetrahydrofolate
-
competitive, multisite inhibition
tetrahydrofolate
-
competitive inhibition
tRNAfMet
-
tRNAfMet from Streptococcus faecalis or E. coli K12, strong inhibition
tRNAfMet
-
non-aminoacylated tRNAfMet is a competitive inhibitor
methotrexate
-
0.01 mM: 30% inhibition, 0.1 mM, 52% inhibition, competitive
additional information
-
inhibition studies, not inhibited by trimethoprim; not inhibited by folic acid
-
additional information
-
not inhibited by folic acid; not inhibited by pteroic acid, aminopterin, methionyl-tRNAmMet and uncharged tRNAmMet
-
additional information
-
E. coli A19 enzyme is not inhibited by uncharged tRNAmMet and tRNAfMet from E. coli K12 or Streptococcus faecalis
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
not stimulated by ATP or GTP
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.006
0.007
10-formyltetrahydrofolate
-
-
0.0133
-
10-formyltetrahydrofolate
-
-
0.0135
-
10-formyltetrahydrofolate
-
-
0.011
0.016
10-formyltetrahydropteroyltriglutamate
-
-
4e-05
-
bovine mitochondrial methionyl-tRNA
-
-
-
0.0003
-
E. coli isoleucyl-tRNAfMet
-
-
-
0.0003
-
E. coli isoleucyl-tRNAfMet
-
-
-
0.01
-
E. coli methionyl-tRNA1Val(CAU)
-
above
-
0.0001
-
E. coli methionyl-tRNAfMet
-
-
-
0.0003
-
E. coli methionyl-tRNAfMet
-
-
-
0.0005
-
E. coli methionyl-tRNAfMet
-
-
-
0.0005
-
E. coli methionyl-tRNAfMet
P23882
-
-
0.00112
-
E. coli methionyl-tRNAfMet
-
-
-
9.7e-05
-
E. coli methionyl-tRNAmMet
-
-
-
0.01
-
E. coli methionyl-tRNAmMet
-
above
-
0.0005
-
E. coli valyl-tRNAfMet
-
-
-
0.0014
-
E. coli valyl-tRNAfMet
-
-
-
0.00035
-
methionyl-tRNAfMet
-
-
-
0.00051
-
methionyl-tRNAfMet
-
wild-type enzyme
-
0.00054
-
methionyl-tRNAfMet
-
wild-type enzyme
-
0.00056
-
methionyl-tRNAfMet
-
-
-
0.0006
-
methionyl-tRNAfMet
-
-
-
0.00066
-
methionyl-tRNAfMet
-
G41R mutant enzyme
-
0.00072
0.0009
methionyl-tRNAfMet
-
-
-
0.00072
-
methionyl-tRNAfMet
-
G178E mutant enzyme
-
0.00102
-
methionyl-tRNAfMet
-
G41K mutant enzyme
-
0.00121
-
methionyl-tRNAfMet
-
R38K mutant enzyme
-
0.00162
-
methionyl-tRNAfMet
-
G41L mutant enzyme
-
0.0017
-
methionyl-tRNAfMet
-
-
-
0.003
-
methionyl-tRNAfMet
-
G41D mutant enzyme
-
0.00324
-
methionyl-tRNAfMet
-
R38L mutant enzyme
-
0.0037
-
methionyl-tRNAfMet
P23882
MTFDeltaC20
-
0.00834
-
methionyl-tRNAfMet
-
G41R/R42L double mutant enzyme
-
0.00866
-
methionyl-tRNAfMet
-
R42K mutant enzyme
-
0.009
-
methionyl-tRNAfMet
-
R42L mutant enzyme
-
0.0096
-
methionyl-tRNAfMet
-
R42Q mutant enzyme
-
0.0013
-
phenylalanyl-tRNAfMet
-
-
8.6e-05
-
tRNAfMet
-
pH 7.5
0.00119
-
tRNAfMet
-
pH 7.5
0.0014
-
valyl-tRNAfMet
-
-
0.01
-
methionyl-tRNAMet
-
-
-
additional information
-
additional information
-
kinetic parameters of the formylation of various mutant methionyl-tRNAs
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetic parameters of the formylation of various mutant methionyl-tRNAs
-
additional information
-
additional information
-
values for wild-type and mutant enzyme with wild-type and mutant initiator tRNAs
-
additional information
-
additional information
P23882
values for several mutant enzymes in the linker region and C-terminal domain
-
additional information
-
additional information
-
kinetic parameters of the formylation of various mutant methionyl-tRNAs
-
additional information
-
additional information
-
values for several mutant enzymes
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0005
-
E. coli isoleucyl-tRNAfMet
-
-
-
0.03
-
E. coli methionyl-tRNA1Val(CAU)
-
above
-
0.13
-
E. coli methionyl-tRNAfMet
-
-
-
0.93
-
E. coli methionyl-tRNAfMet
-
-
-
11.3
-
E. coli methionyl-tRNAfMet
-
-
-
0.04
-
E. coli methionyl-tRNAmMet
-
above
-
0.009
-
E. coli valyl-tRNAfMet
-
-
-
0.2
-
methionyl-tRNAfMet
P23882
MTFDeltaC20
-
0.45
-
methionyl-tRNAfMet
-
G41R/R42L double mutant enzyme
-
0.483
-
methionyl-tRNAfMet
-
R42L mutant enzyme
-
3.1
-
methionyl-tRNAfMet
-
R42Q mutant enzyme
-
8.27
-
methionyl-tRNAfMet
-
R38L mutant enzyme
-
8.9
-
methionyl-tRNAfMet
-
G178E mutant enzyme
-
11.4
-
methionyl-tRNAfMet
-
G41R mutant enzyme
-
13.9
-
methionyl-tRNAfMet
-
wild-type enzyme
-
14.6
-
methionyl-tRNAfMet
-
G41K mutant enzyme
-
20
-
methionyl-tRNAfMet
-
-
-
20
-
methionyl-tRNAfMet
-
+ 10-formyltetrahydrofolate
-
27.7
-
methionyl-tRNAfMet
-
R42K mutant enzyme
-
31.5
-
methionyl-tRNAfMet
-
G41L mutant enzyme
-
33
-
methionyl-tRNAfMet
-
G41D mutant enzyme
-
37.3
-
methionyl-tRNAfMet
P23882
wild-type enzyme
-
39.1
-
methionyl-tRNAfMet
-
wild-type enzyme
-
41.5
-
methionyl-tRNAfMet
-
-
-
46.3
-
methionyl-tRNAfMet
-
R38K mutant enzyme
-
additional information
-
additional information
-
kinetic parameters of the formylation of various mutant methionyl-tRNAs
-
additional information
-
additional information
-
kinetic parameters of the formylation of various mutant methionyl-tRNAs
-
additional information
-
additional information
-
values for wild-type and mutant enzyme with wild-type and mutant initiator tRNAs
-
additional information
-
additional information
P23882
values for several mutant enzymes in the linker region and C-terminal domain
-
additional information
-
additional information
-
kinetic parameters of the formylation of various mutant methionyl-tRNAs
-
additional information
-
additional information
-
values for several mutant enzymes
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.045
-
5-formyltetrahydrofolate
-
-
0.003
-
5-methyltetrahydrofolate
-
-
0.0002
-
tetrahydrofolate
-
-
0.024
-
tetrahydrofolate
-
-
0.00018
0.00057
tRNAfMet
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.013
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
P23882
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
with abrupt decrease of reaction rate below pH 7.0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8
-
good activity between
6.8
8.4
-
about 60% of maximal activity at pH 6.8 and 8.4
7
-
-
below: rapid decrease in reaction rate
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
higher specific activity in isolated chloroplasts than in the remainder of the leaf extract
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
both the methionyl-tRNA formyltransferase and peptide deformylase are localized to the apicoplast only
Manually annotated by BRENDA team
-
both the methionyl-tRNA formyltransferase and peptide deformylase are localized to the apicoplast only
-
Manually annotated by BRENDA team
Euglena gracilis Z
-
-
-
Manually annotated by BRENDA team
Enterococcus faecalis R, Escherichia coli A19
-
-
-
Manually annotated by BRENDA team
Escherichia coli K12 EM20031(F32)
-
;
-
Manually annotated by BRENDA team
Escherichia coli K12 MO
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae D243-2B-R1
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25000
-
-
high speed equilibrium sedimentation
29900
-
-
sucrose density gradient centrifugation
30000
-
-
sedimentation equilibrium method
33000
-
-
sedimentation equilibrium method, gel filtration, small-angle neutron scattering
34000
-
-
gel filtration, small-angle neutron scattering
38000
-
-
gel filtration
45000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 40000, SDS-PAGE
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 32000
monomer
Escherichia coli K12 EM20031(F32)
-
1 * 32000, SDS-PAGE; 1 * 32000, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of enzyme complexed with formylmethionyl-tRNAfMet
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
EDTA or 2-mercaptoethanol stabilizes
-
high ionic strength, e.g. 150 mM KCl stabilizes and prevents adsorption to glassware
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Glycerol
-
50%, stable to
Glycerol
Escherichia coli K12 EM20031(F32)
-
50%, stable to
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, 20 mM imidazole-HCl buffer, pH 7.6, 0.1 mM EDTA, 10 mM 2-mercaptoethanol, 50% glycerol, 150 mM KCl, several months, stable
-
-20C, 1 month, 30% loss of activity
-
-20C, 20 mM imidazole, 10 mM 2-mercaptoethanol, 50% glycerol, 150 mM KCl, stable
-
-20C, 20 mM imidazole, pH 7.5, 10 mM 2-mercaptoethanol, 50% glycerol, 150 mM KCl, 2-4 months, stable
-
-20C, 20 mM imidazole-HCl buffer, pH 7.6, 0.1 mM EDTA, 10 mM 2-mercaptoethanol, 50% glycerol, 150 mM KCl, 6 months, stable
-
25C, 20 mM imidazole-HCl buffer, pH 7.6, 0.1 mM EDTA, 10 mM 2-mercaptoethanol, 150 mM KCl, 2 days, stable
-
-20C, longer than 4 months, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purification of His-tagged recombinant enzyme, expressed in Escherichia coli BL21(DE3)
-
100-300fold, partial purification
-
10000fold purification; affinity chromatography on Sepharose-bound tRNA
-
14fold purification of recombinant wild-type enzyme, overexpressed in Escherichia coli Novablue, purification of His-tagged G178E mutant enzyme
-
affinity chromatography on Sepharose-bound tRNA
-
over 1500fold purification
-
purification of His-tagged wild-type and C-terminal deletion mutant recombinant enzymes, expressed in Escherichia coli
P23882
purification of wild-type and of R42K, R42L and G41R/R42L mutant recombinant enzymes, expressed in Escherichia coli JM109
-
purification of wild-type enzyme and G41R, G41K mutant enzymes
-
1000fold purification from autotrophic cells, 650fold from chloroplasts
-
purification of His6-tagged wild-type and mutant recombinant enzymes, expressed in Escherichia coli BL21(DE3)
-
purification of recombinant enzyme, expressed in Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene encoding mitochondrial enzyme is cloned and expressed in Escherichia coli BL21(DE3) as His-tagged enzyme
-
expression of wild-type and of R42K, R42L and G41R/R42L mutant enzymes in Escherichia coli JM109 as His6-tagged proteins
-
fmt gene encoding MTF is cloned and sequenced, expression in Escherichia coli JM109 as His6-tagged enzyme
-
gene encoding MTF is cloned and sequenced, expression of wild-type and mutant enzymes in Escherichia coli
P23882
wild-type and mutant fmt gene encoding MTF is cloned, overexpression of wild-type enzyme in Escherichia coli Novablue
-
cloning of the fmt gene and expression of wild-type and mutant genes in Escherichia coli BL21(DE3) as His6-tagged proteins
-
expression in Escherichia coli
-
fmt gene encoding enzyme is cloned
-
cloning and expression of the gene encoding mitochondrial enzyme in Escherichia coli Pal13Tr-pMAF and in yeast, several strains lacking gene exhibit in minimal medium a thermosensitive respiratory growth and a slower growth rate
-
fmt gene encoding enzyme is cloned
-
possesses a single gene coding for each FMT and peptide deformylase, PDF, respectively, and both gene products are predicted to carry a bipartite targeting signal
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
G41D
-
mutant enzyme with decreased activity
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
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
G41L
-
mutant enzyme with decreased activity
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
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
Escherichia coli CA274
-
no suppressor mutation
-
G178D
Escherichia coli CA274
-
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
Escherichia coli CA274
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors
-
G178K
Escherichia coli CA274
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors than G178E
-
G178L
Escherichia coli CA274
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors than G178E
-
G41D
Escherichia coli CA274
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41K
Escherichia coli CA274
-
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
Escherichia coli CA274
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41Q
Escherichia coli CA274
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41R
Escherichia coli CA274
-
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
Escherichia coli DH5AlphaF
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41K
Escherichia coli DH5AlphaF
-
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
Escherichia coli DH5AlphaF
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41Q
Escherichia coli DH5AlphaF
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41R
Escherichia coli DH5AlphaF
-
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
Escherichia coli JM109
-
no suppressor mutation
-
G178D
Escherichia coli JM109
-
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
Escherichia coli JM109
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors
-
G178K
Escherichia coli JM109
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors than G178E
-
G178L
Escherichia coli JM109
-
suppressor mutation, compensates for the formylation defect of a mutant elongator lysine-tRNAmMet, G178D, G178K and G178L are progressively weaker suppressors than G178E
-
G41D
Escherichia coli JM109
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41K
Escherichia coli JM109
-
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
Escherichia coli JM109
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41Q
Escherichia coli JM109
-
no suppressor mutation, mutant is stably overproduced in Escherichia coli CA274
-
G41R
Escherichia coli JM109
-
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
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
G41R
-
G41R/R42L double mutant with low activity, G41R: decreased activity
additional information
P23882
several C-terminal deletion mutants and substitution mutants in the linker region between the C- and N-terminal domain and the C-terminal domain
K37A
-
mutant enzyme with 3.5fold reduced formylation rate, kinetic parameters
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
del833
-
inactivated methionyl-tRNA formyltransferase
additional information
-
insertionally inactivated methionyl-tRNA formyltransferase in mutant CDR1 and mutant CDR2
deltafmt1
-
in combination with mutation of AEP3, a gene encodes for a peripheral mitochondrial inner membrane protein, respiratory defect
additional information
P32785, -
mutation analysis shows that methionyl-tRNA-formyltransferase Fmt1p, is essential for respiratory growth in the absence of mitochondrial ribosomal protein Rsm28p