出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/05/05 08:49:16」(JST)
| N-Formylmethionine | |
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IUPAC name
(S)-2-Formylamino-4-methylsulfanylbutanoic acid |
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Other names
2-Formylamino-4-methylsulfanyl-butyric acid; Formylmethionine; N-Formyl(methyl)homocysteine |
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| Identifiers | |
| CAS number | 4289-98-9 |
| PubChem | 911 |
| EC number | 224-322-8 |
| Jmol-3D images | Image 1 |
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SMILES
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| Properties | |
| Molecular formula | C6H11NO3S |
| Molar mass | 177.22 g mol−1 |
| Supplementary data page | |
| Structure and properties |
n, εr, etc. |
| Thermodynamic data |
Phase behaviour Solid, liquid, gas |
| Spectral data | UV, IR, NMR, MS |
| Y (verify) (what is: Y/N?) Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa) |
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| Infobox references | |
N-Formylmethionine (fMet) is a proteinogenic amino acid found in Bacteria and related Prokaryotic organelles. It is a derivative of the amino acid methionine in which a formyl group has been added to the amino group. It is specifically used for initiation of protein synthesis, and may be removed after.
fMet plays a crucial part in the protein synthesis of bacteria, mitochondria and chloroplasts. It is not used in cytosolic protein synthesis of eukaryotes, where eukaryotic nuclear genes are translated. It is also not used by Archaea. In the human body, fMet is recognized by the immune system as foreign material and stimulates the body to fight against potential infection.
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fMet is a starting residue in the synthesis of proteins in bacteria, and, consequently, is located at the N-terminus of the growing polypeptide. fMet is delivered to the ribosome (30S) - mRNA complex by a specialized tRNA (tRNAfMet) which has a 3'-UAC-5' anticodon that is capable of binding with the 5'-AUG-3' start codon located on the mRNA.
fMet is coded by the same codon as methionine, AUG. However, AUG is also the translation initiation codon. When the codon is used for initiation, fMet is used instead of methionine, thereby forming the first amino acid of the nascent peptide chain. When the same codon appears later in the mRNA, normal methionine is used. Many organisms use variations of this basic mechanism.
The addition of the formyl group to methionine is catalyzed by the enzyme methionyl-tRNA formyltransferase. This modification is done after methionine has been loaded onto tRNAfMet by aminoacyl-tRNA synthetase.
Note that methionine can be loaded either onto tRNAfMet or tRNAMet. However, transformylase will catalyze the addition of the formyl group to methionine only if methionine has been loaded onto tRNAfMet and not onto tRNAMet.
This methionine is removed from majority of proteins (both host and recombinant) by methionine aminopeptidase (MAP).[1]
Because fMet is present in proteins made by prokaryotes but not in those made by eukaryotes, the immune system can use it to help distinguish self from non-self. Polymorphonuclear cells can bind proteins starting with N-Formylmethionine, and use them to initiate phagocytosis.[2][3][4]
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| リンク元 | 「ホルミルメチオニン」「fMet」 |
| 拡張検索 | 「N-formylmethionine leucyl-phenylalanine」「N-formylmethionine」 |