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IUBMB Comments Highly specific for N -formylmethionyl peptides. Will not cleave methionyl peptides or N -formyl derivatives of amino acids other than methionine. Isolated from rat liver. Inhibited by heavy metals and activated by Cl-
Reaction Schemes
release of an N-terminal, formyl-methionyl residue from a polypeptide
Synonyms
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(fMet)-releasing enzyme
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Aminopeptidase, formylmethionine
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Formylmethionine aminopeptidase
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release of an N-terminal, formyl-methionyl residue from a polypeptide
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hydrolysis of peptide bond
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Acetyl-Met-Leu + H2O
?
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Substrates: -
?
Acetyl-Met-Leu-Phe + H2O
?
-
Substrates: -
?
Formylnorleucine-Leu-Phe + H2O
?
-
Substrates: -
?
N-Formyl-Met 2-naphthylamide + H2O
N-Formyl-Met + 2-naphthylamine
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Substrates: -
?
N-Formyl-Met-Leu + H2O
N-Formyl-Met + Leu
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Substrates: -
?
N-Formyl-Met-Leu-Phe + H2O
N-Formyl-Met + Leu-Phe
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Substrates: -
?
N-Formyl-Met-Leu-Tyr + H2O
N-Formyl-Met + Leu-Tyr
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Substrates: -
?
N-Formyl-Met-Phe + H2O
N-Formyl-Met + Phe
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Substrates: -
?
N-Formyl-Met-Trp + H2O
N-Formyl-Met + Trp
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Substrates: -
?
N-Formyl-Met-Val + H2O
N-Formyl-Met + Val
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Substrates: -
?
N-Formylmethionyl oligopeptides + H2O
?
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Substrates: the presence of this enzyme in intestinal mucosa can prevent absorption of intact bioactive potent inflammatory N-formylmethionyl oligopeptides produced by commensal bacteria in the gut lumen
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Natural formylmethionine oligopeptide from E. coli culture supernatants + H2O
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Substrates: loss of bioactivity and immuno-reactivity
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additional information
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Substrates: highly specific for N-formyl-Met peptides, will not cleave methionyl peptides or N-formyl derivatives of amino acids other than methionine
?
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N-Formylmethionyl oligopeptides + H2O
?
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Substrates: the presence of this enzyme in intestinal mucosa can prevent absorption of intact bioactive potent inflammatory N-formylmethionyl oligopeptides produced by commensal bacteria in the gut lumen
?
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Cl-
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activates
Cl-
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maximal activity at 1 M
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phenylmethanesulfonyl fluoride
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weak
Cu2+
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moderate
Fe2+
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moderate
additional information
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not: EDTA
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additional information
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2-mercaptoethanol; DTT; N3-; not: EDTA
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0.16
Acetyl-Met-Leu-Phe
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0.23
Formylnorleucine-Leu-Phe
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0.2 - 1.7
N-Formyl-Met 2-naphthylamide
0.03 - 0.04
N-Formyl-Met-Leu
0.18
N-Formyl-Met-Leu-Phe
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-
0.22
N-Formyl-Met-Leu-Tyr
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0.63
N-Formyl-Met-Phe
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0.71
N-Formyl-Met-Trp
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0.06
N-Formyl-Met-Val
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0.2
N-Formyl-Met 2-naphthylamide
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1.7
N-Formyl-Met 2-naphthylamide
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0.03
N-Formyl-Met-Leu
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0.04
N-Formyl-Met-Leu
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-
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27.1
Acetyl-Met-Leu-Phe
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76.4 - 230
N-Formyl-Met 2-naphthylamide
5.17
N-Formyl-Met-Leu
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12.3
N-Formyl-Met-Leu-Phe
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15.5
N-Formyl-Met-Leu-Tyr
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70.2
N-Formyl-Met-Phe
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31.3
N-Formyl-Met-Trp
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5.94
N-Formyl-Met-Val
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76.4
N-Formyl-Met 2-naphthylamide
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230
N-Formyl-Met 2-naphthylamide
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-
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additional information
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6 - 10
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6: about 40% of activity maximum, 10: about 50% of activity maximum
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brenda
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lowest level in oesophagus and stomach and a shallow diminishing gradient from proximal small intestine to distal colon and rectum
brenda
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brenda
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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290000
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rat, gel filtration
72000
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4 * 72000, SDS-PAGE
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tetramer
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4 * 72000, SDS-PAGE
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Suda, H.; Yamamoto, K.; Aoyagi, T.; Umezawa, H.
Purification and properties of N-formylmethionine aminopeptidase from rat liver
Biochim. Biophys. Acta
616
60-67
1980
Rattus norvegicus
brenda
Sherriff, R.M.; Broom, M.F.; Chadwick, V.S.
Isolation and purification of N-formylmethionine aminopeptidase from rat intestine
Biochim. Biophys. Acta
1119
275-280
1992
Rattus norvegicus
brenda
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