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Kynurenine—oxoglutarate Transaminase
In enzymology, a kynurenine-oxoglutarate transaminase () is an enzyme that catalyzes the chemical reaction :-kynurenine + 2-oxoglutarate 4-(2-aminophenyl)-2,4-dioxobutanoate + -glutamate Thus, the two substrates of this enzyme are -kynurenine and 2-oxoglutarate, whereas its two products are 4-(2-aminophenyl)-2,4-dioxobutanoate and -glutamate. The former product is an unstable α-oxo acid that quickly undergoes intramolecular cyclization to form kynurenic acid. This enzyme belongs to the family of transferases, to be specific, the transaminases, that transfer nitrogenous groups. The systematic name of this enzyme class is -kynurenine:2-oxoglutarate aminotransferase. Other names in common use include kynurenine transaminase (cyclizing), kynurenine 2-oxoglutarate transaminase, kynurenine aminotransferase, and -kynurenine aminotransferase. This enzyme participates in tryptophan metabolism Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
GOT2
Aspartate aminotransferase, mitochondrial is an enzyme that in humans is encoded by the ''GOT2'' gene. Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2, respectively. GOT plays a role in amino acid metabolism and the urea and Kreb's cycle. Also, GOT2 is a major participant in the malate-aspartate shuttle, which is a passage from the cytosol to the mitochondria. The two enzymes are homodimeric and show close homology. GOT2 has been seen to have a role in cell proliferation, especially in terms of tumor growth. Structure GOT2 is a dimer containing two identical subunits that hold overlapping subunit regions. The top and sides of the enzyme are made up of helices, while the bottom is formed by strands of beta sheets and extended hairpin loops. The subunit itself can be categorized into four different parts: a large domain, which binds pyridoxal-P, a small domain, an NH2-te ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
KYAT3
Kynurenine aminotransferase 3 is an enzyme that in humans is encoded by the ''KYAT3'' gene. It is one of the Kynurenine—oxoglutarate transaminase In enzymology, a kynurenine-oxoglutarate transaminase () is an enzyme that catalyzes the chemical reaction :-kynurenine + 2-oxoglutarate 4-(2-aminophenyl)-2,4-dioxobutanoate + -glutamate Thus, the two substrates of this enzyme are -kynurenin ...s. References {{enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AADAT
Aadat ( ur, عادت; ) is a Pakistani drama serial directed by Adnan Wai Qureshi, written by Aliya Bukhari and produced by Cereal Entertainment. It originally aired on TVOne. Cast * Anum Fayyaz as Sana * Junaid Khan as Azar * Shermeen Ali as Minaal * Ali Safina as Farhan * Adil Murad as Sarmad * Irsa Ghazal as Neelam * Azra Mohyeddin as Nayyar * Ayub Khoso Ayub Khoso ( ur, ; born 1959) is a Pakistani actor of film and TV. With a career spanning more than three decades - mostly in television - Khoso is a well-known name in Pakistan. He is known for his roles in films like ''Khuda Kay Liye''. Ear ... as Ghazi, Minaal's uncle References Pakistani drama television series 2016 Pakistani television series debuts 2017 Pakistani television series endings Urdu-language television shows TVOne Pakistan {{Pakistan-tv-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
KYAT1
Kynurenine—oxoglutarate transaminase 1 is an enzyme that in humans is encoded by the ''CCBL1'' gene. It is one of the Kynurenine—oxoglutarate transaminases. This gene encodes a cytosolic enzyme which is responsible for the metabolism of cysteine Cysteine (symbol Cys or C; ) is a semiessential proteinogenic amino acid with the formula . The thiol side chain in cysteine often participates in enzymatic reactions as a nucleophile. When present as a deprotonated catalytic residue, sometime ... conjugates of certain halogenated alkenes and alkanes. This metabolism leads to the formation of reactive metabolites which can lead to nephrotoxicity and neurotoxicity. References External links * Further reading * * * * * * * * * * * * * {{gene-9-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pyridoxal Phosphate
Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates. Role as a coenzyme PLP acts as a coenzyme in all transamination reactions, and in certain decarboxylation, deamination, and racemization reactions of amino acids. The aldehyde group of PLP forms a Schiff-base linkage (internal aldimine) with the ε-amino group of a specific lysine group of the aminotransferase enzyme. The α-amino group of the amino acid substrate displaces the ε-amino group of the active-site lysine residue in a process known as transaldimination. The resulting ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cofactor (biochemistry)
A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction). Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound. Cofactors can be divided into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mostly derived from vitamins and other organic essential nutrients in small amounts. (Note that some scientists limit the use of the term "cofactor" for inorganic substances; both types are included here.) Coenzymes are further divided into two types. The first is called a "prosthetic group", which consists of a coenzyme that is tightly (or even covalently) and permanently bound to a protein. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tryptophan Metabolism
Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent. It is essential in humans, meaning that the body cannot synthesize it and it must be obtained from the diet. Tryptophan is also a precursor to the neurotransmitter serotonin, the hormone melatonin, and vitamin B3. It is encoded by the codon UGG. Like other amino acids, tryptophan is a zwitterion at physiological pH where the amino group is protonated (–; pKa = 9.39) and the carboxylic acid is deprotonated ( –COO−; pKa = 2.38). Humans and many animals cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acid. Function Amino acids, including tryptophan, are used as building blocks in protein biosynthesis, and proteins are required to sustain life. Many anima ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
