Phosphoribosylformylglycinamidine Synthase
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Phosphoribosylformylglycinamidine Synthase
In enzymology, a phosphoribosylformylglycinamidine synthase () is an enzyme that catalyzes the chemical reaction :ATP + ''N''2-formyl-''N''1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O \rightleftharpoons ADP + phosphate + 2-(formamido)-''N''1-(5-phospho-D-ribosyl)acetamidine + L-glutamate The 4 substrates of this enzyme are ATP, N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide, L-glutamine, and H2O, whereas its 4 products are ADP, phosphate, 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine, and L-glutamate. This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide:L-glutamine amido-ligase (ADP-forming). Other names in common use include phosphoribosylformylglycinamidine synthetase, formylglycinamide ribonucloetide amidotransferase, phosphoribosylformylglycineamidine synthetase, FGAM syn ...
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Enzymology
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ...
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2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine
A coxless pair is a rowing boat used in the sport of competitive rowing. It is designed for two rowers, who propel the boat with sweep oars. The crew consists of a pair of rowers, each having one oar, one on the stroke side (rower's right hand side) and one on the bow side (rower's lefthand side). As the name suggests, there is no coxswain on such a boat, and the two rowers must co-ordinate steering and the proper timing of oar strokes between themselves or by means of a steering installation which is operated by foot from one of the rowers. The equivalent boat when it is steered by a cox is referred to as a "coxed pair". Racing boats (often called "shells") are long, narrow, and broadly semi-circular in cross-section in order to reduce drag to a minimum. Originally made from wood, shells are now almost always made from a composite material (usually carbon-fibre reinforced plastic) for strength and weight advantages. Pairs have a fin towards the rear, to help prevent rol ...
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Purine Metabolism
Purine metabolism refers to the metabolic pathways to synthesize and break down purines that are present in many organisms. Biosynthesis Purines are biologically synthesized as nucleotides and in particular as ribotides, i.e. bases attached to ribose 5-phosphate. Both adenine and guanine are derived from the nucleotide inosine monophosphate (IMP), which is the first compound in the pathway to have a completely formed purine ring system. IMP Inosine monophosphate is synthesized on a pre-existing ribose-phosphate through a complex pathway (as shown in the figure on the right). The source of the carbon and nitrogen atoms of the purine ring, 5 and 4 respectively, come from multiple sources. The amino acid glycine contributes all its carbon (2) and nitrogen (1) atoms, with additional nitrogen atoms from glutamine (2) and aspartic acid (1), and additional carbon atoms from formyl groups (2), which are transferred from the coenzyme tetrahydrofolate as 10-formyltetrahydrofolate, and a ...
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Protein Data Bank
The Protein Data Bank (PDB) is a database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids. The data, typically obtained by X-ray crystallography, NMR spectroscopy, or, increasingly, cryo-electron microscopy, and submitted by biologists and biochemists from around the world, are freely accessible on the Internet via the websites of its member organisations (PDBe, PDBj, RCSB, and BMRB). The PDB is overseen by an organization called the Worldwide Protein Data Bank, wwPDB. The PDB is a key in areas of structural biology, such as structural genomics. Most major scientific journals and some funding agencies now require scientists to submit their structure data to the PDB. Many other databases use protein structures deposited in the PDB. For example, SCOP and CATH classify protein structures, while PDBsum provides a graphic overview of PDB entries using information from other sources, such as Gene ontology. History Two force ...
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Tertiary Structure
Protein tertiary structure is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure.Branden C. and Tooze J. "Introduction to Protein Structure" Garland Publishing, New York. 1990 and 1991. A number of tertiary structures may fold into a quaternary structure.Kyte, J. "Structure in Protein Chemistry." Garland Publishing, New York. 1995. History The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of polypept ...
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PubMed
PubMed is a free search engine accessing primarily the MEDLINE database of references and abstracts on life sciences and biomedical topics. The United States National Library of Medicine (NLM) at the National Institutes of Health maintain the database as part of the Entrez system of information retrieval. From 1971 to 1997, online access to the MEDLINE database had been primarily through institutional facilities, such as university libraries. PubMed, first released in January 1996, ushered in the era of private, free, home- and office-based MEDLINE searching. The PubMed system was offered free to the public starting in June 1997. Content In addition to MEDLINE, PubMed provides access to: * older references from the print version of ''Index Medicus'', back to 1951 and earlier * references to some journals before they were indexed in Index Medicus and MEDLINE, for instance ''Science'', ''BMJ'', and ''Annals of Surgery'' * very recent entries to records for an article before it ...
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Saccharomyces Cerevisiae
''Saccharomyces cerevisiae'' () (brewer's yeast or baker's yeast) is a species of yeast (single-celled fungus microorganisms). The species has been instrumental in winemaking, baking, and brewing since ancient times. It is believed to have been originally isolated from the skin of grapes. It is one of the most intensively studied eukaryotic model organisms in molecular biology, molecular and cell biology, much like ''Escherichia coli'' as the model bacteria, bacterium. It is the microorganism behind the most common type of fermentation (biochemistry), fermentation. ''S. cerevisiae'' cells are round to ovoid, 5–10 micrometre, μm in diameter. It reproduces by budding. Many proteins important in human biology were first discovered by studying their Homology (biology), homologs in yeast; these proteins include cell cycle proteins, signaling proteins, and protein-processing enzymes. ''S. cerevisiae'' is currently the only yeast cell known to have Berkeley body, Berkeley bo ...
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List Of Enzymes
This article lists enzymes by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system. * List of EC numbers (EC 5) * List of EC numbers (EC 6) :Oxidoreductases (EC 1) (Oxidoreductase) *Dehydrogenase * Luciferase *DMSO reductase :EC 1.1 (act on the CH-OH group of donors) * :EC 1.1.1 (with NAD+ or NADP+ as acceptor) ** Alcohol dehydrogenase (NAD) ** Alcohol dehydrogenase (NADP) **Homoserine dehydrogenase ** Aminopropanol oxidoreductase **Diacetyl reductase **Glycerol dehydrogenase **Propanediol-phosphate dehydrogenase ** glycerol-3-phosphate dehydrogenase (NAD+) ** D-xylulose reductase **L-xylulose reductase **Lactate dehydrogenase **Malate dehydrogenase **Isocitrate dehydrogenase ** HMG-CoA reductase * :EC 1.1.2 (with a cytochrome as acceptor) * :EC 1.1.3 (with oxygen as acceptor) **Glucose oxidase **L-gulonolactone oxidase **Thiamine oxidase **Xanthine oxidase * :EC 1.1.4 (with a disul ...
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Ligase
In biochemistry, a ligase is an enzyme that can catalyze the joining (ligation) of two large molecules by forming a new chemical bond. This is typically via hydrolysis of a small pendant chemical group on one of the larger molecules or the enzyme catalyzing the linking together of two compounds, e.g., enzymes that catalyze joining of C-O, C-S, C-N, etc. In general, a ligase catalyzes the following reaction: :Ab + C → A–C + b or sometimes :Ab + cD → A–D + b + c + d + e + f where the lowercase letters can signify the small, dependent groups. Ligase can join two complementary fragments of nucleic acid and repair single stranded breaks that arise in double stranded DNA during replication. Nomenclature The common names of ligases often include the word "ligase", such as DNA ligase, an enzyme commonly used in molecular biology laboratories to join together DNA fragments. Other common names for ligases include the word "synthetase", because they are used to synthes ...
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L-glutamate
Glutamic acid (symbol Glu or E; the ionic form is known as glutamate) is an α-amino acid that is used by almost all living beings in the biosynthesis of proteins. It is a non-essential nutrient for humans, meaning that the human body can synthesize enough for its use. It is also the most abundant excitatory neurotransmitter in the vertebrate nervous system. It serves as the precursor for the synthesis of the inhibitory gamma-aminobutyric acid (GABA) in GABA-ergic neurons. Its molecular formula is . Glutamic acid exists in three optically isomeric forms; the dextrorotatory -form is usually obtained by hydrolysis of gluten or from the waste waters of beet-sugar manufacture or by fermentation.Webster's Third New International Dictionary of the English Language Unabridged, Third Edition, 1971. Its molecular structure could be idealized as HOOC−CH()−()2−COOH, with two carboxyl groups −COOH and one amino group −. However, in the solid state and mildly acidic water solutio ...
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Phosphate
In chemistry, a phosphate is an anion, salt, functional group or ester derived from a phosphoric acid. It most commonly means orthophosphate, a derivative of orthophosphoric acid . The phosphate or orthophosphate ion is derived from phosphoric acid by the removal of three protons . Removal of one or two protons gives the dihydrogen phosphate ion and the hydrogen phosphate ion ion, respectively. These names are also used for salts of those anions, such as ammonium dihydrogen phosphate and trisodium phosphate. File:3-phosphoric-acid-3D-balls.png, Phosphoricacid File:2-dihydrogenphosphate-3D-balls.png, Dihydrogenphosphate File:1-hydrogenphosphate-3D-balls.png, Hydrogenphosphate File:0-phosphate-3D-balls.png, Phosphate In organic chemistry, phosphate or orthophosphate is an organophosphate, an ester of orthophosphoric acid of the form where one or more hydrogen atoms are replaced by organic groups. An example is trimethyl phosphate, . The term also refers to the triv ...
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Enzyme
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ...
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