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Lyase Inhibitors
In biochemistry, a lyase is an enzyme that catalyzes the breaking (an elimination reaction) of various chemical bonds by means other than hydrolysis (a substitution reaction) and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible (called a Michael reaction). For example, an enzyme that catalyzed this reaction would be a lyase: : ATP → cAMP + PPi Lyases differ from other enzymes in that they require only one substrate for the reaction in one direction, but two substrates for the reverse reaction. Nomenclature Systematic names are formed as "''substrate group-lyase''." Common names include decarboxylase, dehydratase, aldolase, etc. When the product is more important, synthase may be used in the name, e.g. phosphosulfolactate synthase (EC 4.4.1.19, Michael addition of sulfite to phosphoenolpyruvate). A combination of both an elimination and a Michael addition is seen in O-succinylhomoserine (thiol)-lyase (MetY or MetZ) which ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biochemistry
Biochemistry or biological chemistry is the study of chemical processes within and relating to living organisms. A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology and metabolism. Over the last decades of the 20th century, biochemistry has become successful at explaining living processes through these three disciplines. Almost all areas of the life sciences are being uncovered and developed through biochemical methodology and research. Voet (2005), p. 3. Biochemistry focuses on understanding the chemical basis which allows biological molecules to give rise to the processes that occur within living cells and between cells, Karp (2009), p. 2. in turn relating greatly to the understanding of tissues and organs, as well as organism structure and function.Miller (2012). p. 62. Biochemistry is closely related to molecular biology, which is the study of the molecular mechanisms of biological phenomena.Ast ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Synthase
In biochemistry, a synthase is an enzyme that catalyses a synthesis process. Note that, originally, biochemical nomenclature distinguished synthetases and synthases. Under the original definition, synthases do not use energy from nucleoside triphosphates (such as ATP, GTP, CTP, TTP, and UTP), whereas synthetases do use nucleoside triphosphates. However, the Joint Commission on Biochemical Nomenclature (JCBN) dictates that 'synthase' can be used with any enzyme that catalyzes synthesis (whether or not it uses nucleoside triphosphates), whereas 'synthetase' is to be used synonymously with 'ligase'. Examples * ATP synthase * Citrate synthase * Tryptophan synthase * Pseudouridine synthase * Fatty acid synthase Fatty acid synthase (FAS) is an enzyme that in humans is encoded by the ''FASN'' gene. Fatty acid synthase is a multi-enzyme protein that catalyzes fatty acid synthesis. It is not a single enzyme but a whole enzymatic system composed of two ide ... * Cellulose synthase ( ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
List Of EC Numbers (EC 4)
This list contains a list of EC numbers for the fourth group, EC 4, lyases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. EC 4.1: Carbon-Carbon Lyases EC 4.1.1: Carboxy-lyases * : pyruvate decarboxylase * : oxalate decarboxylase * EC 4.1.1.3: Now recognized to be two enzymes xaloacetate decarboxylase (Na+ extruding)and (oxaloacetate decarboxylase). * : acetoacetate decarboxylase * : acetolactate decarboxylase * : ''cis''-aconitate decarboxylase * : benzoylformate decarboxylase * : oxalyl-CoA decarboxylase * : malonyl-CoA decarboxylase * EC 4.1.1.10: Now included with , aspartate 4-decarboxylase * : aspartate 1-decarboxylase * : aspartate 4-decarboxylase * EC 4.1.1.13: deleted * : valine decarboxylase * : glutamate decarboxylase * : hydroxyglutam ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Membranome Database
Membranome database provides structural and functional information about more than 6000 single-pass (bitopic) transmembrane proteins from ''Homo sapiens'', ''Arabidopsis thaliana'', ''Dictyostelium discoideum'', ''Saccharomyces cerevisiae'', ''Escherichia coli'' and ''Methanocaldococcus jannaschii''. Bitopic membrane proteins consist of a single transmembrane alpha-helix connecting water-soluble domains of the protein situated at the opposite sides of a biological membrane. These proteins are frequently involved in the signal transduction and communication between cells in multicellular organisms. The database provides information about the individual proteins including computationally generated three-dimensional models of their transmembrane alpha-helices spatially arranged in the membrane, topology, intracellular localizations, amino acid sequences, domain architecture, functional annotation and available experimental structures from the Protein Data Bank. It also provides ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transmembrane Helix
A transmembrane domain (TMD) is a membrane-spanning protein domain. TMDs generally adopt an alpha helix topological conformation, although some TMDs such as those in porins can adopt a different conformation. Because the interior of the lipid bilayer is hydrophobic, the amino acid residues in TMDs are often hydrophobic, although proteins such as membrane pumps and ion channels can contain polar residues. TMDs vary greatly in length, sequence, and hydrophobicity, adopting organelle-specific properties. Functions of transmembrane domains Transmembrane domains are known to perform a variety of functions. These include: * Anchoring transmembrane proteins to the membrane. *Facilitating molecular transport of molecules such as ions and proteins across biological membranes; usually hydrophilic residues and binding sites in the TMDs help in this process. *Signal transduction across the membrane; many transmembrane proteins, such as G protein-coupled receptors, receive extracellul ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peripheral Membrane Protein
Peripheral membrane proteins, or extrinsic membrane proteins, are membrane proteins that adhere only temporarily to the biological membrane with which they are associated. These proteins attach to integral membrane proteins, or penetrate the peripheral regions of the lipid bilayer. The regulatory protein subunits of many ion channels and transmembrane receptors, for example, may be defined as peripheral membrane proteins. In contrast to integral membrane proteins, peripheral membrane proteins tend to collect in the water-soluble component, or fraction, of all the proteins extracted during a protein purification procedure. Proteins with GPI anchors are an exception to this rule and can have purification properties similar to those of integral membrane proteins. The reversible attachment of proteins to biological membranes has shown to regulate cell signaling and many other important cellular events, through a variety of mechanisms. For example, the close association between many e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biological Membranes
A biological membrane, biomembrane or cell membrane is a selectively permeable membrane that separates the interior of a cell from the external environment or creates intracellular compartments by serving as a boundary between one part of the cell and another. Biological membranes, in the form of eukaryotic cell membranes, consist of a phospholipid bilayer with embedded, integral and peripheral proteins used in communication and transportation of chemicals and ions. The bulk of lipids in a cell membrane provides a fluid matrix for proteins to rotate and laterally diffuse for physiological functioning. Proteins are adapted to high membrane fluidity environment of the lipid bilayer with the presence of an annular lipid shell, consisting of lipid molecules bound tightly to the surface of integral membrane proteins. The cell membranes are different from the isolating tissues formed by layers of cells, such as mucous membranes, basement membranes, and serous membranes. Compositi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ferrochelatase
Protoporphyrin ferrochelatase (EC 4.98.1.1, formerly EC 4.99.1.1, or ferrochelatase; systematic name protoheme ferro-lyase (protoporphyrin-forming)) is an enzyme encoded by the FECH gene in humans. Ferrochelatase catalyses the eighth and terminal step in the biosynthesis of heme, converting protoporphyrin IX into heme B. It catalyses the reaction: :protoheme + 2 H+ = protoporphyrin + Fe2+ Function Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX in the heme biosynthesis pathway to form heme B. The enzyme is localized to the matrix-facing side of the inner mitochondrial membrane. Ferrochelatase is the best known member of a family of enzymes that add divalent metal cations to tetrapyrrole structures. For example, magnesium chelatase adds magnesium to protoporphyrin IX in the first step of bacteriochlorophyll biosynthesis. Heme B is an essential cofactor in many proteins and enzymes. In particular, heme b plays a key role as the oxygen carrie ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Guanylyl Cyclase
Guanylate cyclase (EC 4.6.1.2, also known as guanyl cyclase, guanylyl cyclase, or GC; systematic name GTP diphosphate-lyase (cyclizing; 3′,5′-cyclic-GMP-forming)) is a lyase enzyme that converts guanosine triphosphate (GTP) to cyclic guanosine monophosphate (cGMP) and pyrophosphate: : GTP = 3′,5′-cyclic GMP + diphosphate It is often part of the G protein signaling cascade that is activated by low intracellular calcium levels and inhibited by high intracellular calcium levels. In response to calcium levels, guanylate cyclase synthesizes cGMP from GTP. cGMP keeps cGMP-gated channels open, allowing for the entry of calcium into the cell. Like cAMP, cGMP is an important second messenger that internalizes the message carried by intercellular messengers such as peptide hormones and nitric oxide and can also function as an autocrine signal. Depending on cell type, it can drive adaptive/developmental changes requiring protein synthesis. In smooth muscle, cGMP is the signa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adenylyl Cyclase
Adenylate cyclase (EC 4.6.1.1, also commonly known as adenyl cyclase and adenylyl cyclase, abbreviated AC) is an enzyme with systematic name ATP diphosphate-lyase (cyclizing; 3′,5′-cyclic-AMP-forming). It catalyzes the following reaction: :ATP = 3′,5′-cyclic AMP + diphosphate It has key regulatory roles in essentially all cells. It is the most polyphyletic known enzyme: six distinct classes have been described, all catalyzing the same reaction but representing unrelated gene families with no known sequence or structural homology. The best known class of adenylyl cyclases is class III or AC-III (Roman numerals are used for classes). AC-III occurs widely in eukaryotes and has important roles in many human tissues. All classes of adenylyl cyclase catalyse the conversion of adenosine triphosphate (ATP) to 3',5'-cyclic AMP (cAMP) and pyrophosphate.Magnesium ions are generally required and appear to be closely involved in the enzymatic mechanism. The cAMP produced by AC ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aldehyde Lyases
Fructose-bisphosphate aldolase (), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism. The word aldolase also refers, more generally, to an enzyme that performs an aldol reaction (creating an aldol) or its reverse (cleaving an aldol), such as Sialic acid aldolase, which forms sialic acid. See the list of aldolases. Mechanism and structure Class I proteins form a protonated Schiff base intermediate linking a highly conserved active site lysine with the DHAP carbonyl carbon. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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