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Formylation
In biochemistry, the addition of a formyl functional group is termed formylation. A formyl functional group consists of a carbonyl bonded to hydrogen. When attached to an R group, a formyl group is called an aldehyde. Formylation has been identified in several critical biological processes. Methionine was first discovered to be formylated in ''E. coli'' by Marcker and Sanger in 1964 and was later identified to be involved in the initiation of protein synthesis in bacteria and organelles. The formation of ''N''-formylmethionine is catalyzed by the enzyme methionyl-tRNA transformylase. Additionally, two formylation reactions occur in the de novo biosynthesis of purines. These reactions are catalyzed by the enzymes glycinamide ribonucleotide (GAR) transformylase and 5-aminoimidazole-4-carboxyamide ribotide (AICAR) transformylase. More recently, formylation has been discovered to be a histone modification, which may modulate gene expression. General formylation reaction Formyla ...
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Formyl Functional Group
In organic chemistry, an aldehyde () is an organic compound containing a functional group with the structure . The functional group itself (without the "R" side chain) can be referred to as an aldehyde but can also be classified as a formyl group. Aldehydes are common and play important roles in the technology and biological spheres. Structure and bonding Aldehydes feature a carbon center that is connected by a double bond to oxygen and a single bond to hydrogen and single bond to a third substituent, which is carbon or, in the case of formaldehyde, hydrogen. The central carbon is often described as being sp2- hybridized. The aldehyde group is somewhat polar. The C=O bond length is about 120-122 picometers. Physical properties and characterization Aldehydes have properties that are diverse and that depend on the remainder of the molecule. Smaller aldehydes are more soluble in water, formaldehyde and acetaldehyde completely so. The volatile aldehydes have pungent odors. Aldehy ...
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Aldehyde
In organic chemistry, an aldehyde () is an organic compound containing a functional group with the structure . The functional group itself (without the "R" side chain) can be referred to as an aldehyde but can also be classified as a formyl group. Aldehydes are common and play important roles in the technology and biological spheres. Structure and bonding Aldehydes feature a carbon center that is connected by a double bond to oxygen and a single bond to hydrogen and single bond to a third substituent, which is carbon or, in the case of formaldehyde, hydrogen. The central carbon is often described as being sp2- hybridized. The aldehyde group is somewhat polar. The C=O bond length is about 120-122 picometers. Physical properties and characterization Aldehydes have properties that are diverse and that depend on the remainder of the molecule. Smaller aldehydes are more soluble in water, formaldehyde and acetaldehyde completely so. The volatile aldehydes have pungent odors. Al ...
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Gattermann–Koch Reaction
The Gattermann reaction, (also known as the Gattermann formylation and the Gattermann salicylaldehyde synthesis) is a chemical reaction in which aromatic compounds are formylated by a mixture of hydrogen cyanide (HCN) and hydrogen chloride (HCl) in the presence of a Lewis acid catalyst such as AlCl3. It is named for the German chemist Ludwig Gattermann and is similar to the Friedel–Crafts reaction. Modifications have shown that it is possible to use sodium cyanide or cyanogen bromide in place of hydrogen cyanide. The reaction can be simplified by replacing the HCN/AlCl3 combination with zinc cyanide. Although it is also highly toxic, Zn(CN)2 is a solid, making it safer to work with than gaseous HCN. The Zn(CN)2 reacts with the HCl to form the key HCN reactant and Zn(Cl)2 that serves as the Lewis-acid catalyst ''in-situ''. An example of the Zn(CN)2 method is the synthesis of mesitaldehyde from mesitylene. Gattermann–Koch reaction The Gattermann–Koch reaction, nam ...
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Methanofuran
Methanofurans are a family of chemical compounds found in methanogenic archaea. These species feature a 2-aminomethylfuran linked to phenoxy group. At least three different end groups are recognized: R = tricarboxyheptanoyl (methanofuran), glutamyl-glutamyl (methanofuran b), tricarboxy-2-hydroxyheptanoyl (methanofuran c, see picture). Formylation of MFR Methanofuran converts to formylmethanofuran in an early stage of methanogenesis. The enzyme formylmethanofuran dehydrogenase ( EC: 1.2.99.5) formylates methanofuran using , the primary C1 source in methanogenesis. Deformylation of MFR The enzyme formylmethanofuran:tetrahydromethanopterin formyltransferase catalyzes the transfer of the formyl group from formylmethanofuran to N5 on tetrahydromethanopterin, . This enzyme has been crystallized; it contains no prosthetic group A prosthetic group is the non-amino acid component that is part of the structure of the heteroproteins or conjugated proteins, being tightly linked to t ...
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GAR Transformylase
Phosphoribosylglycinamide formyltransferase (, ''2-amino-N-ribosylacetamide 5'-phosphate transformylase'', ''GAR formyltransferase'', ''GAR transformylase'', ''glycinamide ribonucleotide transformylase'', ''GAR TFase'', ''5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide ribonucleotide transformylase'') is an enzyme with systematic name ''10-formyltetrahydrofolate:5'-phosphoribosylglycinamide N-formyltransferase''. This enzyme catalyses the following chemical reaction : 10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide \rightleftharpoons tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide This THF dependent enzyme catalyzes a nucleophilic acyl substitution of the formyl group from 10-formyltetrahydrofolate (fTHF) to N1-(5-phospho-D-ribosyl)glycinamide (GAR) to form N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide (fGAR) as shown above. This reaction plays an important role in the formation of purine through the ''de novo'' purine biosynthesis pa ...
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AICAR Transformylase
In enzymology, a phosphoribosylaminoimidazolecarboxamide formyltransferase (), also known by the shorter name AICAR transformylase, is an enzyme that catalyzes the chemical reaction :10-formyltetrahydrofolate + AICAR \rightleftharpoons tetrahydrofolate + FAICAR Thus, the two substrates of this enzyme are 10-formyltetrahydrofolate and AICAR, whereas its two products are tetrahydrofolate and FAICAR. This enzyme participates in purine metabolism and one carbon pool by folate. Nomenclature This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 10-formyltetrahydrofolate:5-phosphoribosyl-5-amino-4-imidazole-carb oxamide N-formyltransferase. Other names in common use include: * 10-formyltetrahydrofolate:5-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase * 5-amino-1-ribosyl-4-imidazolecarboxamide 5-phosphate, * 5-amino-4-imi ...
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Initiation Factor
Initiation factors are proteins that bind to the small subunit of the ribosome during the initiation of translation, a part of protein biosynthesis. Initiation factors can interact with repressors to slow down or prevent translation. They have the ability to interact with activators to help them start or increase the rate of translation. In bacteria, they are simply called IFs (i.e.., IF1, IF2, & IF3) and in eukaryotes they are known as eIFs (i.e.., eIF1, eIF2, eIF3). Translation initiation is sometimes described as three step process by which initiation factors help to carry out. First, the tRNA carrying a methionine amino acid binds to the small ribosome, then binds to the mRNA, and finally joining together with the large ribosome. The initiation factors that help with this process each have different roles and structures. Types The initiation factors are divided into three major groups by taxonomic domains. There are some homologies shared (click the domain names to see the ...
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Formyl-methionyl-tRNA
''N''-Formylmethionine (fMet, HCO-Met, For-Met) 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 from bacterial and organellar genes, and may be removed post-translationally. 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, or as an alarm signal released by damaged cells, and stimulates the body to fight against potential infection. Function in protein synthesis 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 (tRNAfM ...
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30S Ribosomal Subunit
The prokaryotic small ribosomal subunit, or 30 S subunit, is the smaller subunit of the 70S ribosome found in prokaryotes. It is a complex of the 16S ribosomal RNA (rRNA) and 19 proteins. This complex is implicated in the binding of transfer RNA to messenger RNA (mRNA). The small subunit is responsible for the binding and the reading of the mRNA during translation. The small subunit, both the rRNA and its proteins, complexes with the large 50S subunit to form the 70S prokaryotic ribosome in prokaryotic cells. This 70S ribosome is then used to translate mRNA into proteins. Function The 30S subunit is an integral part of mRNA translation. It binds three prokaryotic initiation factors: IF-1, IF-2, and IF-3. A portion of the 30S subunit (the 16S rRNA) guides the initiating start codon (5′)-AUG-(3′) of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. This ensures the ribosome start ...
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Methionine Aminopeptidase
Methionyl aminopeptidase (, ''methionine aminopeptidase'', ''peptidase M'', ''L-methionine aminopeptidase'', ''MAP'') is an enzyme. This enzyme catalyses the following chemical reaction : Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides This membrane-bound enzymatic activity is present in both prokaryotes and eukaryotes. Proteins possessing this activity include METAP1 and METAP2 Methionine aminopeptidase 2 is an enzyme that in humans is encoded by the ''METAP2'' gene. Methionine aminopeptidase 2, a member of the dimetallohydrolase family, is a cytosolic metalloenzyme that catalyzes the hydrolytic removal of N-terminal m .... References External links * {{Portal bar, Biology, border=no EC 3.4.11 ...
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Peptide Deformylase
In enzymology, a peptide deformylase () is an enzyme that catalyzes the chemical reaction :H2O + formyl-L-methionyl peptide \rightleftharpoons methionyl peptide + formate Thus, the two substrates of this enzyme are formyl-L-methionyl peptide and H2O, whereas its two products are formate and methionyl peptide. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is formyl-L-methionyl peptide amidohydrolase. Structural studies As of late 2007, 34 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and . See also *Actinonin Actinonin is a naturally occurring antibacterial agent that has demonstrated anti-tumor activity. Actiononin has been shown to inhibit the enzyme peptide deformylase, which is essential in prokaryote A prokaryote () is a sing ...
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