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Terpene Synthase N 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 N 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 N terminal domain has feature of the copalyl diphosphate synthase (CPS) active site. Structure The N-terminal domain forms an alpha-barrel similar to that of the sesquiterpene cyclase epiaristolochene synthase. 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 (C10) synthases, sesquiterpene (C15) synthases and the diterpe ...
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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 ...
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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 ...
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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 ...
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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 ...
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S-linalool Synthase
The enzyme ''S''-linalool synthase (EC 4.2.3.25) catalyzes the chemical reaction :geranyl diphosphate + H2O \rightleftharpoons (3''S'')-linalool + 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 3''S'')-linalool-forming''. Other names in common use include LIS, Lis, and 3''S''-linalool synthase. References * * * EC 4.2.3 Enzymes of unknown structure {{4.2-enzyme-stub ...
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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 ...
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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 ...
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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 ...
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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 ...
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Kaurene Synthase A
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 of this enzyme class is (+)-copalyl-diphosphate lyase (decyclizing). This enzyme participates in diterpenoid 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 5.5.1 Enzymes of unknown structure {{isomerase-stub ...
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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 ...
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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 ...
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