Terpene Synthase C Terminal Domain
In molecular biology, this protein domain belongs to the terpene synthase family (TPS). Its role is to synthesize terpenes, which are part of primary metabolism, such as sterols and carotene, and also part of the secondary metabolism. This entry will focus on the C terminal domain of the TPS protein. Function Terpenes synthases have a role in producing important molecules in metabolism, these molecules are part of a large group called terpenoids . In particular, the C terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates. Or in simpler terms, the C terminal aids the synthesis of new molecules. Structure It is thought to have at least two alpha helices. Conservation Sequences containing this protein domain belong to the terpene synthase family. It has been suggested that this gene family be designated tps (for terpene synthase). Sequence comparisons reveal similarities between the monoterpene (C ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Protein Domain
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer aft ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Vetispiridiene Synthase
Vetispiradiene synthase (EC 4.2.3.21) is an enzyme from Egyptian henbane that catalyzes the following chemical reaction: :(2''E'',6''E'')-farnesyl diphosphate \rightleftharpoons vetispiradiene + diphosphate This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is (2''E'',6''E'')-farnesyl-diphosphate diphosphate-lyase (cyclizing, vetispiradiene-forming). Other names in common use include vetispiradiene-forming farnesyl pyrophosphate cyclase, pemnaspirodiene synthase, HVS, and vetispiradiene cyclase. This enzyme participates in terpenoid biosynthesis The terpenoids, also known as isoprenoids, are a class of naturally occurring organic chemicals derived from the 5-carbon compound isoprene and its derivatives called terpenes, diterpenes, etc. While sometimes used interchangeably with "terpenes", .... References * * * * * EC 4.2.3 Enzymes of unknown structure {{4.2-enz ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Fungus
A fungus ( : fungi or funguses) is any member of the group of eukaryotic organisms that includes microorganisms such as yeasts and molds, as well as the more familiar mushrooms. These organisms are classified as a kingdom, separately from the other eukaryotic kingdoms, which by one traditional classification include Plantae, Animalia, Protozoa, and Chromista. A characteristic that places fungi in a different kingdom from plants, bacteria, and some protists is chitin in their cell walls. Fungi, like animals, are heterotrophs; they acquire their food by absorbing dissolved molecules, typically by secreting digestive enzymes into their environment. Fungi do not photosynthesize. Growth is their means of mobility, except for spores (a few of which are flagellated), which may travel through the air or water. Fungi are the principal decomposers in ecological systems. These and other differences place fungi in a single group of related organisms, named the ''Eumycota'' (''true f ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Ent-kaurene Synthase B
The enzyme ''ent''-kaurene synthase (EC 4.2.3.19) catalyzes the chemical reaction :''ent''-copalyl diphosphate \rightleftharpoons ''ent''-kaurene + diphosphate This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is ''ent''-copalyl-diphosphate diphosphate-lyase (cyclizing, ''ent''-kaurene-forming). Other names in common use include ''ent''-kaurene synthase B, ''ent''-kaurene synthetase B, ''ent''-copalyl-diphosphate diphosphate-lyase, and (cyclizing). This enzyme participates in diterpenoid biosynthesis. In ''Stevia'' In ''Stevia'' spp., ''ent''-kaurene synthase is a required part of the biosynthesis of steviol. Hajihashemi ''et al.'', 2013 find that it is involved in the drought stress response and because it mimics drought stress paclobutrazol toxicity. Both inhbit transcription Transcription refers to the process of converting sounds (voice, music etc.) into letters or music ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Myrcene Synthase
The enzyme myrcene synthase (EC 4.2.3.15) catalyzes the chemical reaction :geranyl diphosphate \rightleftharpoons myrcene + diphosphate This enzyme belongs to the family of lyase 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. ...s, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is geranyl-diphosphate diphosphate-lyase (myrcene-forming). This enzyme participates in monoterpenoid biosynthesis. References * EC 4.2.3 Enzymes of unknown structure {{4.2-enzyme-stub ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Pinene Synthase
In enzymology, a pinene synthase () is an enzyme that catalyzes the chemical reaction :geranyl diphosphate \rightleftharpoons pinene + diphosphate Hence, this enzyme has one substrate, geranyl diphosphate, and two products, pinene and diphosphate. This enzyme belongs to the family of lyase 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. ...s, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is geranyl-diphosphate diphosphate-lyase (cyclizing, pinene-forming). Other names in common use include beta-geraniolene synthase, (−)-(1S,5S)-pinene synthase, and geranyldiphosphate diphosphate lyase (pinene forming). This enzyme participates in monoterpenoid biosynthesis. References * * * EC 4.2.3 Enzymes of unknown str ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Taxadiene Synthase
The enzyme taxadiene synthase (EC 4.2.3.17) catalyzes the chemical reaction :geranylgeranyl diphosphate \rightleftharpoons taxa-4,11-diene + diphosphate This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivial ... of this enzyme class is geranylgeranyl-diphosphate diphosphate-lyase (cyclizing, taxa-4,11-diene-forming). Other names in common use include geranylgeranyl-diphosphate diphosphate-lyase (cyclizing, and taxadiene-forming). This enzyme participates in diterpenoid biosynthesis. References * * * * * EC 4.2.3 Enzymes of unknown structure {{4.2-enzyme-stub ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Copalyl Diphosphate Synthase
In enzymology, a copalyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction :geranylgeranyl diphosphate \rightleftharpoons (+)-copalyl diphosphate Hence, this enzyme has one substrate, geranylgeranyl diphosphate, and one product, (+)-copalyl diphosphate. This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivial ... of this enzyme class is (+)-copalyl-diphosphate lyase (decyclizing). This enzyme participates in diterpenoid biosynthesis. References * * * * * EC 5.5.1 Enzymes of unknown structure {{isomerase-stub ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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(-)-limonene Synthase
The enzyme (4''S'')-limonene synthase (EC 4.2.3.16) catalyzes the chemical reaction :geranyl diphosphate \rightleftharpoons (−)-(4''S'')-limonene + diphosphate This enzyme belongs to the family of lyase 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. ...s, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is geranyl-diphosphate diphosphate-lyase yclizing, (−)-(4''S'')-limonene-forming''. Other names in common use include (−)-(4''S'')-limonene synthase, 4''S''-(−)-limonene synthase, geranyldiphosphate diphosphate lyase (limonene forming), geranyldiphosphate diphosphate lyase yclizing,, and (4''S'')-limonene-forming''. This enzyme participates in monoterpenoid biosynthesis. References * * * EC 4.2.3 Enzyme ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Thromboxane-A Synthase
Thromboxane A synthase 1 (, platelet, cytochrome P450, family 5, subfamily A), also known as TBXAS1, is a cytochrome P450 enzyme that, in humans, is encoded by the ''TBXAS1'' gene. Function This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases that catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids, and other lipids. However, this protein is considered a member of the cytochrome P450 superfamily on the basis of sequence similarity rather than functional similarity. This endoplasmic reticulum membrane protein catalyzes the conversion of prostaglandin H2 to thromboxane A2, a potent vasoconstrictor and inducer of platelet aggregation, and also to 12-Hydroxyheptadecatrienoic acid (i.e. 12-(''S'')-hydroxy-5''Z'',8''E'',10''E''-heptadecatrienoic acid or 12-HHT) an agonist of Leukotriene B4 receptors (i.e. BLT2 receptors) and mediator of certain BLT2 receptor actions. The enz ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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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 * Cellulose synthase (UDP-forming) * Cellulose synthase (GDP-forming) In enzymology, a cellulose synthase (GDP-forming) () is an enzyme that catalyzes the chemical reaction :GDP-glucose + (1,4-beta-D-glucosyl)n \rightleftharpoons GDP + (1,4-beta-D-glucosyl)n+1 Thus, the tw ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |