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Ornithine Cyclodeaminase
The enzyme ornithine cyclodeaminase (EC 4.3.1.12) catalyzes the chemical reaction L-ornithine \rightleftharpoons L-proline + NH4+ This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is Lornithine ammonia-lyase (cyclizing; L-proline-forming). Other names in common use include ornithine cyclase, ornithine cyclase (deaminating), and L-ornithine ammonia-lyase (cyclizing). This enzyme participates in arginine and proline biosynthesis. It employs one cofactor, NAD+. Structural studies As of late 2007, two structures A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or system so organized. Material structures include man-made objects such as buildings and machines and natural objects such as ... have been solved for this class of enzymes, with PDB accession codes and . References * * * * * EC 4.3 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Catalysis
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recycles quickly, very small amounts of catalyst often suffice; mixing, surface area, and temperature are important factors in reaction rate. Catalysts generally react with one or more reactants to form intermediates that subsequently give the final reaction product, in the process of regenerating the catalyst. Catalysis may be classified as either homogeneous, whose components are dispersed in the same phase (usually gaseous or liquid) as the reactant, or heterogeneous, whose components are not in the same phase. Enzymes and other biocatalysts are often considered as a third category. Catalysis is ubiquitous in chemical industry of all kinds. Estimates are that 90% of all commercially produced chemical products involve catalysts at some s ... [...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] |
Acta Crystallographica Section D
''Acta Crystallographica'' is a series of peer-reviewed scientific Academic journal, journals, with articles centred on crystallography, published by the International Union of Crystallography (IUCr). Originally established in 1948 as a single journal called ''Acta Crystallographica'', there are now six independent ''Acta Crystallographica'' titles: *''Acta Crystallographica#Acta Crystallographica Section A: Foundations and Advances, Acta Crystallographica Section A: Foundations and Advances'' *''Acta Crystallographica#Acta Crystallographica Section B: Structural Science, Crystal Engineering and Materials, Acta Crystallographica Section B: Structural Science, Crystal Engineering and Materials'' *''Acta Crystallographica#Acta Crystallographica Section C: Structural Chemistry, Acta Crystallographica Section C: Structural Chemistry'' *''Acta Crystallographica#Acta Crystallographica Section D: Structural Biology, Acta Crystallographica Section D: Structural Biology'' *''Acta Crystallogr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biochemistry (journal)
''Biochemistry'' is a peer-reviewed academic journal in the field of biochemistry. Founded in 1962, the journal is now published weekly by the American Chemical Society, with 51 or 52 annual issues. The journal's 2015 impact factor was 2.876, and it received a total of 79,348 citations in 2015.''Biochemistry'': About (accessed May 24, 2017) The previous editor-in-chief was Richard N. Armstrong () (2004–16). After his death, ( |
Proceedings Of The National Academy Of Sciences Of The United States Of America
''Proceedings of the National Academy of Sciences of the United States of America'' (often abbreviated ''PNAS'' or ''PNAS USA'') is a peer-reviewed multidisciplinary scientific journal. It is the official journal of the National Academy of Sciences, published since 1915, and publishes original research, scientific reviews, commentaries, and letters. According to ''Journal Citation Reports'', the journal has a 2021 impact factor of 12.779. ''PNAS'' is the second most cited scientific journal, with more than 1.9 million cumulative citations from 2008 to 2018. In the mass media, ''PNAS'' has been described variously as "prestigious", "sedate", "renowned" and "high impact". ''PNAS'' is a delayed open access journal, with an embargo period of six months that can be bypassed for an author fee ( hybrid open access). Since September 2017, open access articles are published under a Creative Commons license. Since January 2019, ''PNAS'' has been online-only, although print issues are ava ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Journal Of Biological Chemistry
The ''Journal of Biological Chemistry'' (''JBC'') is a weekly peer-reviewed scientific journal that was established in 1905., jbc.org Since 1925, it is published by the American Society for Biochemistry and Molecular Biology. It covers research in areas of biochemistry and molecular biology. The editor is Alex Toker. As of January 2021, the journal is fully open access. In press articles are available free on its website immediately after acceptance. Editors The following individuals have served as editors of the journal: * 1906–1909: John Jacob Abel and Christian Archibald Herter * 1909–1910: Christian Archibald Herter * 1910–1914: Alfred Newton Richards * 1914–1925: Donald D. Van Slyke * 1925–1936: Stanley R. Benedict. After Benedict died, John T. Edsall served as temporary editor until the next editor was appointed. * 1937–1958: Rudolph J. Anderson * 1958–1967: John T. Edsall * 1968–1971: William Howard Stein * 1971–2011: Herbert Tabor * 2011–2015: ... [...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] |
NAD+
Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD and NADH (H for hydrogen), respectively. In metabolism, nicotinamide adenine dinucleotide is involved in redox reactions, carrying electrons from one reaction to another. The cofactor is, therefore, found in two forms in cells: NAD is an oxidizing agent – it accepts electrons from other molecules and becomes reduced. This reaction, also with H+, forms NADH, which can then be used as a reducing agent to donate electrons. These electron transfer reactions are the main function of NAD. However, it is also used in other cellular processes, most notably as a substrate of enzymes in adding or removing chemical groups to ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chemical Reaction
A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the positions of electrons in the forming and breaking of chemical bonds between atoms, with no change to the Atomic nucleus, nuclei (no change to the elements present), and can often be described by a chemical equation. Nuclear chemistry is a sub-discipline of chemistry that involves the chemical reactions of unstable and radioactive Chemical element, elements where both electronic and nuclear changes can occur. The substance (or substances) initially involved in a chemical reaction are called reagent, reactants or reagents. Chemical reactions are usually characterized by a chemical change, and they yield one or more Product (chemistry), products, which usually have properties different from the reactants. Reactions often consist of a sequence o ... [...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] |
Proline
Proline (symbol Pro or P) is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group but is rather a secondary amine. The secondary amine nitrogen is in the protonated form (NH2+) under biological conditions, while the carboxyl group is in the deprotonated −COO− form. The "side chain" from the α carbon connects to the nitrogen forming a pyrrolidine loop, classifying it as a aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting with CC (CCU, CCC, CCA, and CCG). Proline is the only proteinogenic secondary amino acid which is a secondary amine, as the nitrogen atom is attached both to the α-carbon and to a chain of three carbons that together form a five-membered ring. History and etymology Proline was first isolated in 1900 by Richard Willstätter who obtained the amino ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
