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https://en.wikipedia.org/wiki/Pulsed%20radiofrequency | Pulsed radiofrequency is the technique whereby radio frequency (RF) oscillations are gated at a rate of pulses (cycles) per second (one cycle per second is known as a hertz (Hz)). Radio frequency energies occupy to of the electromagnetic spectrum. Radio frequency electromagnetic energy is routinely produced by RF electrical circuits connected to a transducer, usually an antenna.
Pulsed radio frequency waveforms
The figure below shows an example of a generalized pulsed radio frequency waveform as seen with an oscilloscope with an antenna probe. In this example there are 1000 pulses per second (one kilohertz pulse rate) with a gated pulse width of 42 μs. The pulse packet frequency in this example is 27.125 MHz of RF energy. The duty cycle for a pulsed radio frequency is the percent time the RF packet is on, 4.2% for this example ([0.042 ms × 1000 pulses divided by 1000 ms/s] × 100). The pulse packet form can be a square, triangle, sawtooth or sine wave. In several applications of pulse radio frequency, such as radar, times between pulses can be modulated.
Use in radar
The best understood and applied use of pulse radio frequency electromagnetic energy is their use in radar. The uses of radar are diverse and applied to military, civilian and space exploration. Radar is based on the reflection or scatter of pulsed radiofrequency waves emitted from a transmitter which are then detected by an antenna which then determines the range, speed, and direction of objects. In most uses |
https://en.wikipedia.org/wiki/Color%20reaction | In chemistry, a color reaction or colour reaction is a chemical reaction that is used to transform colorless chemical compounds into colored derivatives which can be detected visually or with the aid of a colorimeter.
The concentration of a colorless solution cannot normally be determined with a colorimeter. The addition of a color reagent leads to a color reaction and the absorbance of the colored product can then be measured with a colorimeter.
A change in absorbance in the ultraviolet range cannot be detected by eye but can be measured by a suitably equipped colorimeter. A special colorimeter is required because standard colorimeters cannot operate below a wavelength of 400 nanometers. It is also necessary to use fused quartz cuvettes because glass is opaque to ultraviolet.
Color reagents
Many different color reagents have been developed for determining the concentrations of different substances. For example, Nessler's reagent can be used to determine the concentration of a solution of ammonia.
Thin layer chromatography
In thin layer chromatography (TLC) color reactions are frequently used to detect compound spots by dipping the plate into the reagent or by spraying the reagent onto the plates.
See also
Blood sugar
Colorimeter
Derivatization
MBAS assay
References
Chemical reactions |
https://en.wikipedia.org/wiki/HLA-DPB1 | HLA class II histocompatibility antigen, DP(W2) beta chain is a protein that in humans is encoded by the HLA-DPB1 gene.
HLA-DPB belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DPA) and a beta chain (DPB), both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. Within the DP molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to 4 different molecules.
See also
Major histocompatibility complex
Human leukocyte antigen
HLA-DP
References
Further reading |
https://en.wikipedia.org/wiki/Kitl | Kitl or KITL may refer to:
Kernel Independent Transport Layer
Kittel, a Jewish ritual garment
Stem cell factor, or KIT ligand
KZTN-LD, a low-power television station (channel 20) licensed to serve Boise, Idaho, United States, which held the call sign KITL-LP or KITL-LD from 2002 to 2013
See also
Kjetil, a Norwegian masculine name |
https://en.wikipedia.org/wiki/Keratohyalin | Keratohyalin is a protein structure found in cytoplasmic granules of the keratinocytes in the stratum granulosum of the epidermis. Keratohyalin granules (KHG) mainly consist of keratin, profilaggrin, loricrin and trichohyalin proteins which contribute to cornification or keratinization, the process of the formation of epidermal cornified cell envelope. During the keratinocyte differentiation, these granules maturate and expand in size, which leads to the conversion of keratin tonofilaments into a homogenous keratin matrix, an important step in cornification.
Keratohyalin granules can be divided in three classes: globular KHG (found in quickly dividing epithelia, such as the oral mucose), stellate KHG (found in the slowly dividing normal epidermis) and KHG of Hassall's corpuscles or type VI epithelioreticular cells of the thymus gland. The exact purpose of the keratinization of Hassall's corpuscles remains unknown.
During skin differentiation process, keratohyaline granules discharge their contents in the junction between stratum granulosum and stratum corneum cell layers and form the barrier. At the same time, the inner side of the cell membrane thickens forming the cornified cell envelope. After the release of the granules, nuclei, ribosomes and mitochondria disappear, the cells become densely packaged with filaggrin and cover more surface. After final dehydration, the cell desquamates.
Keratohyalin granules contribute significantly to the process of skin moisturization, |
https://en.wikipedia.org/wiki/Surfactant%20protein%20A1 | Surfactant protein A1 (SP-A1), also known as Pulmonary surfactant-associated protein A1 (PSP-A) is a protein that in humans is encoded by the SFTPA1 gene.
Summary
SP-A1 is primarily synthesised in type II alveolar cells in the lung, as part of a complex of lipids and proteins known as pulmonary surfactant. The function of this complex is to reduce surface tension in the alveoli and prevent their collapse during expiration. The protein component of surfactant helps in the modulation of the innate immune response, and inflammatory processes.
SP-A1 is a member of a subfamily of C-type lectins called collectins. Together with SP-A2, they are the most abundant proteins of pulmonary surfactant. SP-A1 binds to the carbohydrates found in the surface of several microorganisms and helps in the defense against respiratory pathogens.
Surfactant homeostasis is critical for breathing (and thus survival) in the prematurely born infant, but also for maintaining lung health, and normal lung function throughout life. Changes in the amount or composition of surfactant can alter its function and are associated with respiratory diseases.
SFTPA1 expression
The lung is the main site of SFTPA1 synthesis, but SFTPA1 mRNA expression has also been detected in the trachea, prostate, pancreas, thymus, colon, eye, salivary gland and other tissues. Using specific monoclonal antibodies for Surfactant protein A, the protein can be detected in lung alveolar type II pneumocytes, club cells, and alveol |
https://en.wikipedia.org/wiki/Anhydrosialidase | The enzyme anhydrosialidase () catalyzes the following process:
Elimination of α-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-α-N-acetylneuraminate
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is glycoconjugate sialyl-lyase (2,7-cyclizing). Other names in common use include anhydroneuraminidase, sialglycoconjugate N-acylneuraminylhydrolase (2,7-cyclizing), and sialidase L.
References
EC 4.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arabinonate%20dehydratase | The enzyme arabinonate dehydratase () catalyzes the chemical reaction
D-arabinonate 2-dehydro-3-deoxy-D-arabinonate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-arabinonate hydro-lyase (2-dehydro-3-deoxy-D-arabinonate-forming). This enzyme is also called D-arabinonate hydro-lyase.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aristolochene%20synthase | The enzyme aristolochene synthase (EC 4.2.3.9) catalyzes the chemical reaction
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, aristolochene-forming). Other names in common use include sesquiterpene cyclase, trans,trans-farnesyl diphosphate aristolochene-lyase, ''trans,trans''-farnesyl-diphosphate diphosphate-lyase (cyclizing and aristolochene-forming). This enzyme participates in terpenoid biosynthesis.
This protein may use the morpheein model of allosteric regulation.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and . They are both notable for the very high helix content of the structure.
References
EC 4.2.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Arogenate%20dehydratase | Arogenate dehydratase (ADT) () is an enzyme that catalyzes the chemical reaction
L-arogenate → L phenylalanine + H2O + CO2
Certain forms of the protein have the potential to catalyze a second reaction,
L-prephenate → L-phenylpyruvate + H2O + CO2
This enzyme participates in phenylalanine, tyrosine, and tryptophan biosynthesis (an example structure is shown to the right.
Nomenclature
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming). Other names in common use include:
arogenate dehydratase
L-arogenate hydro-lyase (decarboxylating)
cyclohexadienyl dehydratase
carbocyclohexadienyl dehydratase
pheC
ADT
Reaction
The carboxyl and hydroxide groups (shown in red) attached to the 2,5-cyclohexene ring are eliminated from L-arogenate, leaving as carbon dioxide and water. The 2,5-cyclohexene ring becomes a phenyl ring, and L-phenylalanine is formed.
Certain forms of ADT have been shown to exhibit some prephenate dehydratase (PDT) activity in addition to the standard ADT activity described above. Known as cyclohexadienyl dehydratases or carbocyclohexadienyl dehydratases (listed above), these forms of the enzyme catalyze the same type of reaction (a decarboxylation and a dehydration) on prephenate. The carboxyl and hydroxide groups (in red) attached to the 2,5-cyclohexene ring are removed, leaving phenylpyru |
https://en.wikipedia.org/wiki/ATP-dependent%20NAD%28P%29H-hydrate%20dehydratase | The enzyme ATP-dependent NAD(P)H-hydrate dehydratase () catalyzes the chemical reactions
ATP + (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide ADP + phosphate + NADH
ATP + (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate ADP + phosphate + NADPH
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing; NADH-forming). Other names in common use include reduced nicotinamide adenine dinucleotide hydrate dehydratase, ATP-dependent H4NAD(P)+OH dehydratase, (6S)-β-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-, and dinucleotide hydro-lyase (ATP-hydrolysing).
References
EC 4.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Bile-acid%207alpha-dehydratase | The enzyme bile-acid 7α-dehydratase () catalyzes the chemical reaction
7α,12α-dihydroxy-3-oxochol-4-enoate 12α-hydroxy-3-oxochola-4,6-dienoate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 7α,12α-dihydroxy-3-oxochol-4-enoate hydro-lyase (12α-hydroxy-3-oxochola-4,6-dienoate-forming). This enzyme is also called 7α,12α-dihydroxy-3-oxochol-4-enoate hydro-lyase.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carboxymethyloxysuccinate%20lyase | The enzyme carboxymethyloxysuccinate lyase (EC 4.2.99.12) catalyzes the chemical reaction
carboxymethyloxysuccinate fumarate + glycolate
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that cleave carbon-oxygen bonds. The systematic name of this enzyme class is carboxymethyloxysuccinate glycolate-lyase (fumarate-forming). Other names in common use include carbon-oxygen lyase, and carboxymethyloxysuccinate glycolate-lyase.
References
EC 4.2.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carnitine%20dehydratase | In enzymology, a carnitine dehydratase () is an enzyme that catalyzes the chemical reaction
L-carnitine 4-(trimethylammonio)but-2-enoate + H2O
Hence, this enzyme has one substrate, L-carnitine, and two products, 4-(trimethylammonio)but-2-enoate and H2O.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-carnitine hydro-lyase [4-(trimethylammonio)but-2-enoate-forming]. This enzyme is also called L-carnitine hydro-lyase.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Casbene%20synthase | The enzyme casbene synthase (EC 4.2.3.8) catalyzes the chemical reaction
geranylgeranyl diphosphate casbene + 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 geranylgeranyl-diphosphate diphosphate-lyase (cyclizing, casbene-forming). Other names in common use include casbene synthetase, and geranylgeranyl-diphosphate diphosphate-lyase (cyclizing). This enzyme participates in diterpenoid biosynthesis.
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CDP-glucose%204%2C6-dehydratase | The enzyme CDP-glucose 4,6-dehydratase () catalyzes the chemical reaction
CDP-glucose CDP-4-dehydro-6-deoxy-D-glucose + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. This enzyme participates in starch and sucrose metabolism. It employs one cofactor, NAD+.
Nomenclature
The systematic name of this enzyme class is CDP-glucose 4,6-hydro-lyase (CDP-4-dehydro-6-deoxy-D-glucose-forming). Other names in common use include:
cytidine diphosphoglucose oxidoreductase, and
CDP-glucose 4,6-hydro-lyase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 4.2.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Chondroitin%20AC%20lyase | The enzyme chondroitin AC lyase () catalyzes the chemical reaction
Eliminative degradation of polysaccharides containing 1,4-β-D-hexosaminyl and 1,3-β-D-glucuronosyl linkages to disaccharides containing 4-deoxy-β-D-gluc-4-enuronosyl groups
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is chondroitin AC lyase. Other names in common use include chondroitinase (ambiguous), chondroitin sulfate lyase, chondroitin AC eliminase, chondroitin AC lyase, chondroitinase AC, and ChnAC.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
EC 4.2.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Chondroitin%20B%20lyase | The enzyme chondroitin B lyase () catalyzes the following process:
Eliminative cleavage of dermatan sulfate containing (1→4)-β-D-hexosaminyl and (1→3)-β-D-glucurosonyl or (1→3)-α-L-iduronosyl linkages to disaccharides containing 4-deoxy-β-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (ΔUA-GalNAc-4S).
Glossary:
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is chondroitin B lyase. Other names in common use include chondroitinase B, ChonB, and ChnB.
References
EC 4.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chondroitin-sulfate-ABC%20endolyase | The enzyme chondroitin-sulfate-ABC endolyase () catalyzes the following process:
Endolytic cleavage of (1→4)-β-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Δ4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Δ4-unsaturated tetra- and disaccharides
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is chondroitin-sulfate-ABC endolyase. Other names in common use include chondroitinase (ambiguous), chondroitin ABC eliminase (ambiguous), chondroitinase ABC (ambiguous), chondroitin ABC lyase (ambiguous), chondroitin sulfate ABC lyase (ambiguous), ChS ABC lyase (ambiguous), chondroitin sulfate ABC endoeliminase, chondroitin sulfate ABC endolyase, and ChS ABC lyase I.
References
EC 4.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chondroitin-sulfate-ABC%20exolyase | The enzyme chondroitin-sulfate-ABC exolyase () catalyzes the following process:
Exolytic removal of Δ4-unsaturated disaccharide residues from the non-reducing ends of both polymeric chondroitin/dermatan sulfates and their oligosaccharide fragments.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is chondroitin-sulfate-ABC exolyase. Other names in common use include chondroitinase (ambiguous), chondroitin ABC eliminase (ambiguous), chondroitinase ABC (ambiguous), chondroitin ABC lyase (ambiguous), chondroitin sulfate ABC lyase (ambiguous), ChS ABC lyase (ambiguous), chondroitin sulfate ABC exoeliminase, chondroitin sulfate ABC exolyase, and ChS ABC lyase II.
References
EC 4.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chorismate%20synthase | The enzyme chorismate synthase (EC 4.2.3.5) catalyzes the chemical reaction
5-O-(1-carboxyvinyl)-3-phosphoshikimate chorismate + phosphate
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase (chorismate-forming). This enzyme is also called 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
Chorismate synthase catalyzes the last of the seven steps in the shikimate pathway which is used in prokaryotes, fungi and plants for the biosynthesis of aromatic amino acids. It catalyzes the 1,4-trans elimination of the phosphate group from 5-enolpyruvylshikimate-3-phosphate (EPSP) to form chorismate which can then be used in phenylalanine, tyrosine or tryptophan biosynthesis. Chorismate synthase requires the presence of a reduced flavin mononucleotide (FMNH2 or FADH2) for its activity. Chorismate synthase from various sources shows a high degree of sequence conservation. It is a protein of about 360 to 400 amino-acid residues.
Biological and practical function
The shikimate pathway synthesises aromatic amino acids as well as other aromatic compounds that have various involvement with processes such as "UV protection, electron transport, signaling, communication, plant defense, and the wound response".
Moreover, the enzymes catalysing the Shik |
https://en.wikipedia.org/wiki/Citrate%20dehydratase | In enzymology, a citrate dehydratase () is an enzyme that catalyzes the chemical reaction
citrate cis-aconitate + H2O
Hence, this enzyme has one substrate, citrate, and two products, cis-aconitate and H2O.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is citrate hydro-lyase (cis-aconitate-forming). This enzyme is also called citrate hydro-lyase.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Crotonoyl-%28acyl-carrier-protein%29%20hydratase | In enzymology, a crotonoyl-[acyl-carrier-protein] hydratase () is an enzyme that catalyzes the chemical reaction
(3R)-3-hydroxybutanoyl-[acyl-carrier-protein] but-2-enoyl-[acyl-carrier-protein] + H2O
Hence, this enzyme has one substrate, [[(3R)-3-hydroxybutanoyl-[acyl-carrier-protein]]], and two products, [[but-2-enoyl-[acyl-carrier-protein]]] and H2O.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydro-lyase (but-2-enoyl-[acyl-carrier protein]-forming). Other names in common use include (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydro-lyase, beta-hydroxybutyryl acyl carrier protein dehydrase, beta-hydroxybutyryl acyl carrier protein (ACP) dehydrase, beta-hydroxybutyryl acyl carrier protein dehydrase, enoyl acyl carrier protein hydrase, crotonyl acyl carrier protein hydratase, 3-hydroxybutyryl acyl carrier protein dehydratase, beta-hydroxybutyryl acyl carrier, and protein dehydrase. This enzyme participates in fatty acid biosynthesis.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyanamide%20hydratase | The enzyme cyanamide hydratase () catalyzes the chemical reaction
urea cyanamide + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is urea hydro-lyase (cyanamide-forming). This enzyme is also called urea hydro-lyase. This enzyme participates in atrazine degradation.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyanide%20hydratase | The enzyme cyanide hydratase () catalyzes the chemical reaction
formamide cyanide + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is formamide hydro-lyase (cyanide-forming). Other names in common use include formamide dehydratase, and formamide hydro-lyase. This enzyme participates in cyanoamino acid metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclohexa-1%2C5-dienecarbonyl-CoA%20hydratase | The enzyme cyclohexa-1,5-dienecarbonyl-CoA hydratase () catalyzes the chemical reaction
6-hydroxycyclohex-1-enecarbonyl-CoA cyclohexa-1,5-dienecarbonyl-CoA + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 6-hydroxycyclohex-1-enecarbonyl-CoA (cyclohexa-1,5-dienecarbonyl-CoA-forming). Other names in common use include cyclohexa-1,5-diene-1-carbonyl-CoA hydratase, dienoyl-CoA hydratase, and cyclohexa-1,5-dienecarbonyl-CoA hydro-lyase (incorrect). This enzyme participates in benzoate degradation via CoA ligation.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclohexyl-isocyanide%20hydratase | The enzyme cyclohexyl-isocyanide hydratase () catalyzes the chemical reaction
N-cyclohexylformamide cyclohexyl isocyanide + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is N-cyclohexylformamide hydro-lyase (cyclohexyl-isocyanide-forming). Other names in common use include isonitrile hydratase, and ''N''-cyclohexylformamide hydro-lyase. This enzyme participates in caprolactam degradation.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-fuconate%20dehydratase | The enzyme D-fuconate dehydratase () catalyzes the chemical reaction.
D-fuconate 2-dehydro-3-deoxy-D-fuconate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-fuconate hydro-lyase (2-dehydro-3-deoxy-D-fuconate-forming). This enzyme is also called D-fuconate hydro-lyase. This enzyme participates in fructose and mannose metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-glutamate%20cyclase | The enzyme D-glutamate cyclase () catalyzes the chemical reaction
D-glutamate 5-oxo-Dproline + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-glutamate hydro-lyase (cyclizing; 5-oxo-D-proline-forming). This enzyme is also called D-glutamate hydro-lyase (cyclizing). This enzyme participates in D-glutamine and D-glutamate metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydroxy-acid%20dehydratase | The enzyme dihydroxy-acid dehydratase () catalyzes the chemical reaction
2,3-dihydroxy-3-methylbutanoate 3-methyl-2-oxobutanoate + H2O
This enzyme participates in valine, leucine and isoleucine biosynthesis and pantothenate and coenzyme A (CoA) biosynthesis.
Nomenclature
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 2,3-dihydroxy-3-methylbutanoate hydro-lyase (3-methyl-2-oxobutanoate-forming). Other names in common use include
acetohydroxyacid dehydratase,
α,β-dihydroxyacid dehydratase,
2,3-dihydroxyisovalerate dehydratase,
α,β-dihydroxyisovalerate dehydratase,
dihydroxy acid dehydrase,
DHAD,
and 2,3-dihydroxy-acid hydro-lyase.
References
Further reading
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dimethylmaleate%20hydratase | The enzyme dimethylmaleate hydratase () catalyzes the chemical reaction
(2R,3S)-2,3-dimethylmalate dimethylmaleate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (2R,3S)-2,3-dimethylmalate hydro-lyase (dimethylmaleate-forming). This enzyme is also called (2R,3S)-2,3-dimethylmalate hydro-lyase. This enzyme participates in c5-branched dibasic acid metabolism. It employs one cofactor, iron.
References
EC 4.2.1
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DNA-%28apurinic%20or%20apyrimidinic%20site%29%20lyase | The enzyme DNA-(apurinic or apyrimidinic site) lyase, also referred to as DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase (systematic name) or DNA AP lyase (EC 4.2.99.18) catalyzes the cleavage of the C-O-P bond 3' from the apurinic or apyrimidinic site in DNA via β-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. In the 1970s, this class of enzyme was found to repair at apurinic or apyrimidinic DNA sites in E. coli and in mammalian cells. The major active enzyme of this class in bacteria, and specifically, E. coli is endonuclease type III. This enzyme is part of a family of lyases that cleave carbon-oxygen bonds.
Other names for DNA AP lyase include: AP lyase; AP endonuclease class I; endodeoxyribonuclease (apurinic or apyrimidinic); deoxyribonuclease (apurinic or apyrimidinic); E. coli endonuclease III; phage-T4 UV endonuclease; Micrococcus luteus UV endonuclease; AP site-DNA 5'-phosphomonoester-lyase; and X-ray endonuclease III.
Structural studies
Since DNA AP lyase is a class of structures who have numerous target genes that encode for different variations of the enzyme, there is no one single enzyme structure that can be used as an example that encompasses all versions of the enzyme. As of March 2015, 99 structures have been solved for this class of enzymes. Examples from PDB are the accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .
Mechanism
AP lyase enzymes catalyze re |
https://en.wikipedia.org/wiki/D%28-%29-tartrate%20dehydratase | The enzyme D(−)-tartrate dehydratase () catalyzes the chemical reaction
(S,S)-tartrate oxaloacetate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (S,S)-tartrate hydro-lyase (oxaloacetate-forming). Other names in common use include D-tartrate dehydratase, and (S,S)-tartrate hydro-lyase. It has 2 cofactors: iron and manganese.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 4.2.1
Iron enzymes
Manganese enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/DTDP-glucose%204%2C6-dehydratase | The enzyme dTDP-glucose 4,6-dehydratase () catalyzes the chemical reaction
dTDP-glucose dTDP-4-dehydro-6-deoxy-D-glucose + H2O
Structure and mechanism of action
The first protein structures of a dTDP-glucose 4,6-dehydratase (RmlB) were completed by Jim Thoden in the Hazel Holden lab (University of Wisconsin–Madison) and Simon Allard in the Jim Naismith lab (University of St Andrews). Further structural, mutagenic, and enzymatic studies by both groups, along with important mechanistic work by the W. Wallace Cleland and Perry Frey groups have led to a good understanding of this enzyme. In brief summary, the enzyme is a dimeric protein with a Rossmann fold; it uses the tightly bound coenzyme NAD+ for transiently oxidizing the substrate, activating it for the dehydration step.
Nomenclature
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is dTDP-glucose 4,6-hydro-lyase (dTDP-4-dehydro-6-deoxy-D-glucose-forming). Other names in common use include thymidine diphosphoglucose oxidoreductase, TDP-glucose oxidoreductase, RmlB, DESIV, and dTDP-glucose 4,6-hydro-lyase. This enzyme participates in 4 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, polyketide sugar unit biosynthesis, and biosynthesis of vancomycin group antibiotics.
References
Further reading
EC 4.2.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Ectoine%20synthase | The enzyme ectoine synthase () catalyzes the chemical reaction
(2S)-4-acetamido-2-aminobutanoate L-ectoine + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (2S)-4-acetamido-2-aminobutanoate (L-ectoine-forming). Other names in common use include N-acetyldiaminobutyrate dehydratase, ''N-acetyldiaminobutanoate dehydratase, L-ectoine synthase, EctC, and 4-N''-acetyl-L-2,4-diaminobutanoate hydro-lyase (L-ectoine-forming). This enzyme participates in glycine, serine and threonine metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28-%29-endo-fenchol%20synthase | The enzyme (–)-endo-Fenchol synthase (EC 4.2.3.10) catalyzes the chemical reaction
geranyl diphosphate + HO (–)-endo-fenchol + 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 geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-endo-fenchol-forming]. Other names in common use include (−)-endo-fenchol cyclase, and geranyl pyrophosphate:(−)-endo-fenchol cyclase. This enzyme participates in monoterpenoid biosynthesis.
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ent-kaurene%20synthase | The enzyme ent-kaurene synthase (EC 4.2.3.19) catalyzes the chemical reaction
ent-copalyl diphosphate 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 of steviol glycoside synthesis genes including ent-kaurene synthase. This is believed to reduce steviol content in the final plant product.
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ethanolamine-phosphate%20phospho-lyase | The enzyme ethanolamine-phosphate phospho-lyase (EC 4.2.3.2) catalyzes the chemical reaction
ethanolamine phosphate + H2O acetaldehyde + NH3 + phosphate
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is ethanolamine-phosphate phosphate-lyase (deaminating; acetaldehyde-forming). Other names in common use include O-phosphoethanolamine-phospholyase, amino alcohol O-phosphate phospholyase, ''O''-phosphorylethanol-amine phospho-lyase, and ethanolamine-phosphate phospho-lyase (deaminating). It employs one cofactor, pyridoxal phosphate.
References
EC 4.2.3
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Galactarate%20dehydratase | The enzyme galactarate dehydratase () catalyzes the chemical reaction
D-galactarate 5-dehydro-4-deoxy-D-glucarate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-galactarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming). This enzyme is also called D-galactarate hydro-lyase. This enzyme participates in ascorbate and aldarate metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Galactonate%20dehydratase | The enzyme galactonate dehydratase () catalyzes the chemical reaction
D-galactonate 2-dehydro-3-deoxy-D-galactonate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-galactonate hydro-lyase (2-dehydro-3-deoxy-D-alactonate-forming). Other names in common use include D-galactonate dehydrase, D-galactonate dehydratase, and D-galactonate hydro-lyase. This enzyme participates in galactose metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/GDP-mannose%204%2C6-dehydratase | The enzyme GDP-mannose 4,6-dehydratase () catalyzes the chemical reaction
GDP-mannose GDP-4-dehydro-6-deoxy-D-mannose + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is GDP-mannose 4,6-hydro-lyase (GDP-4-dehydro-6-deoxy-D-mannose-forming). Other names in common use include guanosine 5'-diphosphate-D-mannose oxidoreductase, guanosine diphosphomannose oxidoreductase, guanosine diphosphomannose 4,6-dehydratase, GDP-D-mannose dehydratase, GDP-D-mannose 4,6-dehydratase, Gmd, and GDP-mannose 4,6-hydro-lyase. This enzyme participates in fructose and mannose metabolism. It employs one cofactor, NAD+.
GDP-Mannose 4, 6-Dehydratase Reaction
The enzyme GDP-Mannose 4, 6-Dehydratase is in the lyase family of enzymes, specifically the hydro-lyases. Other names in use include guanosine 5'-diphosphate-D-mannose oxidoreductase, guanosine diphosphomannose oxidoreductase, guanosine diphosphomannose 4,6-dehydratase, GDP-D-mannose dehydratase, GDP-D-mannose 4,6-dehydratase, GMD, and GDP-mannose 4,6-hydro-lyase. The enzyme is a part of the GDP-Fucose de novo synthesis pathway and catalyzes the first step in the process that gives us GDP-Fucose which is essential for the transfer of Fucose sugars. Its primary structure contains 372 amino acids. This is an essential enzyme in that fucose plays a major role in cell immunity and signaling. Currently GDP-Mannose 4, 6-Dehydratase is not |
https://en.wikipedia.org/wiki/Germacrene-A%20synthase | The enzyme germacrene-A synthase (EC 4.2.3.23) catalyzes the chemical reaction
(2E,6E)-farnesyl diphosphate (+)-(R)-gemacrene A + 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 (2E,6E)-farnesyl-diphosphate diphosphate-lyase [(+)-(R)-germacrene-A-forming]. Other names in common use include germacrene A synthase, (+)-germacrene A synthase, (+)-(10R)-germacrene A synthase, GAS, 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase, (germacrene-A-forming).
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucarate%20dehydratase | The enzyme glucarate dehydratase () catalyzes the chemical reaction
D-glucarate 5-dehydro-4-deoxy-D-glucarate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-glucarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming). Other names in common use include D-glucarate dehydratase, and D-glucarate hydro-lyase. This enzyme participates in ascorbate and aldarate metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Gluconate%20dehydratase | The enzyme gluconate dehydratase () catalyzes the chemical reaction
D-gluconate 2-dehydro-3-deoxy-D-gluconate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-gluconate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming). Other names in common use include D-gluconate dehydratase, and D-gluconate hydro-lyase. This enzyme participates in the pentose phosphate pathway.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucuronan%20lyase | The enzyme glucuronan lyase () catalyzes the following process:
Eliminative cleavage of (1→4)-β-D-glucuronans to give oligosaccharides with 4-deoxy-β-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is (1→4)-β-D-glucuronan lyase. This enzyme is also called (1,4)-β-D-glucuronan lyase.
References
EC 4.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol%20dehydratase | In enzymology, a glycerol dehydratase () catalyzes the chemical reaction
glycerol 3-hydroxypropanal + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is glycerol hydro-lyase (3-hydroxypropanol-forming). Other names in common use include glycerol dehydrase, and glycerol hydro-lyase. This enzyme participates in glycerolipid metabolism. It employs one cofactor, cobalamin.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 4.2.1
Cobamide enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Heparin%20lyase | The enzyme heparin lyase () catalyzes the following process:
Eliminative cleavage of polysaccharides containing (1→4)-linked D-glucuronate or L-iduronate residues and (1→4)-α-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-α-D-gluc-4-enuronosyl groups at their non-reducing ends
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is heparin lyase. Other names in common use include heparin eliminase, and heparinase.
References
EC 4.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Heparin-sulfate%20lyase | The enzyme heparin-sulfate lyase () catalyzes the chemical reaction
Elimination of sulfate; appears to act on linkages between N-acetyl-D-lucosamine and uronate. Product is an unsaturated sugar.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is heparin-sulfate lyase. Other names in common use include heparin-sulfate eliminase, heparitin-sulfate lyase, heparitinase I, and heparitinase II.
References
EC 4.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Homoaconitate%20hydratase | The enzyme homoaconitate hydratase () catalyzes the chemical reaction
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate (Z)-but-1-ene-1,2,4-tricarboxylate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate hydro-lyase [(Z)-but-1-ene-1,2,4-tricarboxylate-forming]. Other names in common use include homoaconitase, cis-homoaconitase, HACN, Lys4, LysF, and 2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase (incorrect). This enzyme participates in lysine biosynthesis.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hyaluronate%20lyase | The enzyme hyaluronate lyase () catalyzes the chemical reaction
Cleaves hyaluronate chains at a β-D-GalNAc-(1→4)-β-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-β-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is hyaluronate lyase. Other names in common use include hyaluronidase (ambiguous), (hyalurononglucosaminidase) (ambiguous), (hyaluronoglucuronidase)], glucuronoglycosaminoglycan lyase, spreading factor, and mucinase (ambiguous).
Structural studies
As of late 2007, 27 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , and .
References
EC 4.2.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Hydroperoxide%20dehydratase | The enzyme hydroperoxide dehydratase () catalyzes the chemical reaction
(9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate (9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase [(9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate-forming]. Other names in common use include hydroperoxide isomerase, linoleate hydroperoxide isomerase, linoleic acid hydroperoxide isomerase, HPI, (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate, and 12,13-hydro-lyase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Imidazoleglycerol-phosphate%20dehydratase | The enzyme imidazoleglycerol-phosphate dehydratase () catalyzes the chemical reaction
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-erythro-1-(imidazol-4-yl)glycerol-3-phosphate hydro-lyase [3-(imidazol-4-yl)-2-oxopropyl-phosphate-forming]. Other names in common use include IGP dehydratase, and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate hydro-lyase. This enzyme participates in histidine metabolism as it is involved in the 6th step of histidine biosynthesis as part of a nine step cyclical pathway.
There are two isoforms of IGPD; IGPD1 and IGPD2. The different isoforms are highly conserved with only 8 amino acids differing between them. These subtle differences however affect their activity but as yet it is unknown how.
In most organisms IGPD is a monofunctional protein of about 22 to 29 kD. In some bacteria such as Escherichia coli, it is the C-terminal domain of a bifunctional protein that include a histidinol-phosphatase domain. In E. coli, this is the protein encoded by the hisB gene.
Inhibition
Certain compounds that inhibit IGPD have been used as herbicides as animals do not have this protein. One of these inhibitors is 3-Amino-1,2,4-triazole (3-AT), which has also been used as a competitive inhibitor of the product of the yeast HIS3 gene (another IGPD), e. |
https://en.wikipedia.org/wiki/Inulin%20fructotransferase%20%28DFA-I-forming%29 | The enzyme inulin fructotransferase (DFA-I-forming) () catalyzes the following process:
Produces α-D-fructofuranose β-D-fructofuranose 1,2′:2,1′-dianhydride (DFA I) by successively eliminating the diminishing (2→1)-β-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is (2→1)-β-D-fructan lyase (α-Dfructofuranose-β-D-fructofuranose-1,2′:2,1′-dianhydride-forming). Other names in common use include inulin fructotransferase (DFA-I-producing), inulin fructotransferase (depolymerizing,, difructofuranose-1,2':2',1-dianhydride-forming), inulin D-fructosyl-D-fructosyltransferase, (1,2':1',2-dianhydride-forming), inulin D-fructosyl-D-fructosyltransferase (forming, and α-D-fructofuranose β-D-fructofuranose 1,2':1',2-dianhydride).
References
EC 4.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inulin%20fructotransferase%20%28DFA-III-forming%29 | The enzyme inulin fructotransferase (DFA-III-forming) () catalyzes the following process:
Produces α-D-fructofuranose β-D-fructofuranose 1,2′:2,3′-dianhydride (DFA III) by successively eliminating the diminishing (2→1)-β-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
Nomenclature
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is (2→1)-β-D-fructan lyase (α-D-fructofuranose-β-D-fructofuranose-1,2′:2,3′-dianhydride-forming). Other names in common use include inulin fructotransferase (DFA-III-producing), inulin fructotransferase (depolymerizing), inulase II, inulinase II, inulin fructotransferase (depolymerizing, difructofuranose-1,2′:2,3′-dianhydride-forming), inulin D-fructosyl-D-fructosyltransferase, (1,2′:2,3′-dianhydride-forming), inulin D-fructosyl-D-fructosyltransferase (forming, and α-D-fructofuranose β-D-fructofuranose 1,2′:2,3'-dianhydride).
References
EC 4.2.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Isohexenylglutaconyl-CoA%20hydratase | The enzyme isohexenylglutaconyl-CoA hydratase () catalyzes the chemical reaction
3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA 3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA hydro-lyase [3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA-forming]. Other names in common use include 3-hydroxy-3-isohexenylglutaryl-CoA-hydrolase, isohexenylglutaconyl coenzyme A hydratase, β-isohexenylglutaconyl-CoA-hydratase, and 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA hydro-lyase.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isoprene%20synthase | The enzyme isoprene synthase (EC 4.2.3.27) catalyzes the chemical reaction
prenyl pyrophosphate isoprene + 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 prenyl-diphosphate diphosphate-lyase (isoprene-forming). Other names in common use include ISPC, and ISPS.
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Itaconyl-CoA%20hydratase | The enzyme itaconyl-CoA hydratase () catalyzes the chemical reaction
citramalyl-CoA itaconyl-CoA + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is citramalyl-CoA hydro-lyase (itaconyl-CoA-forming). Other names in common use include itaconyl coenzyme A hydratase, and citramalyl-CoA hydro-lyase. This enzyme participates in c5-branched dibasic acid metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Kievitone%20hydratase | The enzyme kievitone hydratase () catalyzes the chemical reaction
kievitone hydrate kievitone + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is kievitone-hydrate hydro-lyase (kievitone-forming). Other names in common use include KHase, and kievitone-hydrate hydro-lyase.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lactoyl-CoA%20dehydratase | The enzyme lactoyl-CoA dehydratase () catalyzes the chemical reaction
lactoyl-CoA acryloyl-CoA + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is lactoyl-CoA hydro-lyase (acryloyl-CoA-forming). Other names in common use include lactoyl coenzyme A dehydratase, lactyl-coenzyme A dehydrase, lactyl CoA dehydratase, acrylyl coenzyme A hydratase, and lactoyl-CoA hydro-lyase. This enzyme participates in propanoate metabolism and styrene degradation.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-arabinonate%20dehydratase | The enzyme L-arabinonate dehydratase () catalyzes the chemical reaction
L-arabinonate 2-dehydro-3-deoxy-L-arabinonate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-arabinonate hydro-lyase (2-dehydro-3-deoxy-L-arabinonate-forming). Other names in common use include L-arabonate dehydrase, L-arabonate dehydratase, and L-arabinonate hydro-lyase. This enzyme participates in ascorbate and aldarate metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Levan%20fructotransferase%20%28DFA-IV-forming%29 | The enzyme levan fructotransferase (DFA-IV-forming) () catalyzes the following process:
Produces di-β-D-fructofuranose 2,6′:2′,6-dianhydride (DFA IV) by successively eliminating the diminishing (2→6)-β-D-fructan (levan) chain from the terminal D-fructosyl-D-fructosyl disaccharide
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is 2→6-β-D-fructan lyase (di-β-D-fructofuranose-2,6′:2′,6-dianhydride-forming).
Other names in common use include 2,6-β-D-fructan D-fructosyl-D-fructosyltransferase (forming, di-β-Dfructofuranose 2,6′:2′,6-dianhydride), and levan fructotransferase.
References
EC 4.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-fuconate%20dehydratase | The enzyme L-fuconate dehydratase () catalyzes the chemical reaction
L-fuconate 2-dehydro-3-deoxy-L-fuconate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-fuconate hydro-lyase (2-dehydro-3-deoxy-L-fuconate-forming). This enzyme is also called L-fuconate hydro-lyase.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Long-chain-enoyl-CoA%20hydratase | The enzyme long-chain-enoyl-CoA hydratase () catalyzes the chemical reaction
(3S)-3-hydroxyacyl-CoA trans-2-enoyl-CoA + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is long-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase. This enzyme is also called long-chain enoyl coenzyme A hydratase. This enzyme participates in fatty acid elongation in mitochondria and fatty acid metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-rhamnonate%20dehydratase | The enzyme Lrhamnonate dehydratase () catalyzes the chemical reaction
L-rhamnonate 2-dehydro-3-deoxy-L-rhamnonate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-rhamnonate hydro-lyase (2-dehydro-3-deoxy-L-rhamnonate-forming). This enzyme is also called Lrhamnonate hydro-lyase. This enzyme participates in fructose and mannose metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/L%28%2B%29-tartrate%20dehydratase | The enzyme L(+)-tartrate dehydratase () catalyzes the chemical reaction
(R,R)-tartrate oxaloacetate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (R,R)-tartrate hydro-lyase (oxaloacetate-forming). Other names in common use include tartrate dehydratase, tartaric acid dehydrase, L-tartrate dehydratase, L-(+)-tartaric acid dehydratase, and (R,R)-tartrate hydro-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It has 2 cofactors: iron, and Thiol.
References
EC 4.2.1
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Maleate%20hydratase | The enzyme maleate hydratase () catalyzes the chemical reaction
(R)-malate maleate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (R)-malate hydro-lyase (maleate-forming). Other names in common use include D-malate hydro-lyase, malease, and (R)-malate hydro-lyase. This enzyme participates in butanoate metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mannonate%20dehydratase | The enzyme mannonate dehydratase () catalyzes the chemical reaction
D-mannonate 2-dehydro-3-deoxy-D-gluconate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is D-mannonate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming). Other names in common use include mannonic hydrolase, mannonate hydrolyase, altronic hydro-lyase, altronate hydrolase, D-mannonate hydrolyase, and D-mannonate hydro-lyase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Methylglyoxal%20synthase | The enzyme methylglyoxal synthase (EC 4.2.3.3) catalyzes the chemical reaction
glycerone phosphate 2-oxopropanal + phosphate
Attempts to observe reversibility of this reaction have been unsuccessful.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is glycerone-phosphate phosphate-lyase (methylglyoxal-forming). Other names in common use include methylglyoxal synthetase, and glycerone-phosphate phospho-lyase. This enzyme participates in pyruvate metabolism and is constitutively expressed.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
Methylglyoxal synthase (MGS) is a 152-amino acid homohexamer that has a molecular weight of approximately 67,000 kD. The total solvent-accessible surface area of the MGS homohexamer is 18,510 square Angstroms, roughly 40% of the total possible surface area if the subunits were separated. Each monomer consists of five alpha helices surrounding five beta sheets. Of these, two antiparallel beta sheets and one alpha helix are located in a subdomain where the N-terminus and C-terminus are in close juxtaposition. The homohexamer exhibits a threefold axis perpendicular to a twofold axis. Within the wide V-groove, there are twelve hydrogen bonds and six salt bridges between the monomers in the presence of phosphate binding. In the absence of phosphate bi |
https://en.wikipedia.org/wiki/Methylthioribulose%201-phosphate%20dehydratase | The enzyme methylthioribulose 1-phosphate dehydratase () catalyzes the chemical reaction
5-(methylsulfanyl)-D)ribulose 1-phosphate 5-(methylthio)-2,3-dioxopentyl phosphate + H2
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 5-methyl-5-thio-D-ribulose-1-phosphate 4-hydro-lyase [5-(methylthio)-2,3-dioxopentyl-phosphate-forming]. Other names in common use include 1-PMT-ribulose dehydratase, and S-methyl-5-thio-D-ribulose-1-phosphate hydro-lyase. This enzyme participates in methionine metabolism.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Myo-inosose-2%20dehydratase | The enzyme myo-inosose-2 dehydratase () catalyzes the chemical reaction
2,4,6/3,5-pentahydroxycyclohexanone 3,5/4-trihydroxycyclohexa-1,2-dione + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 2,4,6/3,5-pentahydroxycyclohexanone hydro-lyase (3,5/4-trihydroxycyclohexa-1,2-dione-forming). Other names in common use include inosose 2,3-dehydratase, ketoinositol dehydratase, and 2,4,6/3,5-pentahydroxycyclohexanone hydro-lyase. This enzyme participates in inositol phosphate metabolism. It has 2 cofactors: manganese, and Cobalt.
References
EC 4.2.1
Manganese enzymes
Cobalt enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Myrcene%20synthase | The enzyme myrcene synthase (EC 4.2.3.15) catalyzes the chemical reaction
geranyl diphosphate myrcene + 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 geranyl-diphosphate diphosphate-lyase (myrcene-forming). This enzyme participates in monoterpenoid biosynthesis.
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Octopamine%20dehydratase | The enzyme octopamine dehydratase () catalyzes the chemical reaction
1-(4-hydroxyphenyl)-2-aminoethanol (4-hydroxyphenyl)acetaldehyde + NH3
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 1-(4-hydroxyphenyl)-2-aminoethanol hydro-lyase [deaminating (4-hydroxyphenyl)acetaldehyde-forming]. Other names in common use include octopamine hydrolyase, and octopamine hydro-lyase (deaminating).
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Oleate%20hydratase | The enzyme oleate hydratase () catalyzes the chemical reaction
(R)-10-hydroxystearate oleate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (R)-10-hydroxystearate 10-hydro-lyase (oleate-forming). This enzyme is also called (R)-10-hydroxystearate 10-hydro-lyase.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Oligogalacturonide%20lyase | The enzyme oligogalacturonide lyase () catalyzes the chemical reaction
4-(4-deoxy-β-D-gluc-4-enuronosyl)-D-galacturonate 2 5-dehydro-4-deoxy-D-glucuronate
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is oligogalacturonide lyase. Other names in common use include oligogalacturonate lyase, unsaturated oligogalacturonate transeliminase, and OGTE. This enzyme participates in pentose and glucuronate interconversions.
References
EC 4.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pectate%20disaccharide-lyase | The enzyme pectate disaccharide-lyase () catalyzes the following process:
(1,4-α-D-galacturonosyl)n = (1,4-α-D-galacturonosyl)n–2 + 4-(4-deoxy-α-D-galact-4-enuronosyl)-D-galacturonate
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is (1→4)-alpha-D-galacturonan reducing-end-disaccharide-lyase. Other names in common use include pectate exo-lyase, exopectic acid transeliminase, exopectate lyase, exopolygalacturonic acid-trans-eliminase, PATE, exo-PATE, and exo-PGL.
References
EC 4.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pectate%20lyase | Pectate lyase () is an enzyme involved in the maceration and soft rotting of plant tissue. Pectate lyase is responsible for the eliminative cleavage of pectate, yielding oligosaccharides with 4-deoxy-α-D-mann-4-enuronosyl groups at their non-reducing ends. The protein is maximally expressed late in pollen development. It has been suggested that the pollen expression of pectate lyase genes might relate to a requirement for pectin degradation during pollen tube growth.
This enzyme catalyzes the chemical reaction
Eliminative cleavage of (1→4)-α-D-galacturonan to give oligosaccharides with 4-deoxy-α-D-galact-4-enuronosyl groups at their non-reducing ends
The structure and the folding kinetics of one member of this family, pectate lyase C (pelC)1 from Erwinia chrysanthemi has been investigated in some detail,. PelC contains a parallel beta-helix folding motif. The majority of the regular secondary structure is composed of parallel beta-sheets (about 30%). The individual strands of the sheets are connected by unordered loops of varying length. The backbone is then formed by a large helix composed of beta-sheets. There are two disulphide bonds in PelC and 12 proline residues. One of these prolines, Pro220, is involved in a cis peptide bond. The folding mechanism of PelC involves two slow phases that have been attributed to proline isomerization.
Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances |
https://en.wikipedia.org/wiki/Pectin%20lyase | Pectin lyase is a polysaccharide enzyme with a complex structure that is present in plant cell walls. It has a significant role in pectin degradation and different biotechnological and industrial applications. It can be found in different organisms.
EC number
The Pectin lyase is an enzyme whose EC number is (EC4.2.2.10). It is a numerical classification system for enzymes based on their catalyzed chemical reactions.
Pectin pathway
Pectin lyase is a component that is found in plant cell walls. This enzyme creates unsaturated products by breaking the glycosidic bonds that are inside. Pectin lyase is critical for several biological processes, such as the maturation of fruits and reshaping of plant cell walls. The enzyme's reaction pathway contains binding to the substrate and active site, splitting of glycosidic bonds, unsaturated products forming, and product release. Pectin lyase is crucial to decaying plant materials and is commonly used in the food industry and biotechnology.
Organisms and function
There are many organisms that contain the pectin enzyme such as plants (Fruits and Vegetables), especially, during fruit maturation, some plants produce internal pectin lyases that lead to the analysis of pectin in cell walls. The citrus, apples, and Pumpkin. The waste residues of citrus, apple, and pomelo and their peels are the major raw resources of pectin production because they are considered by-products of producing juice in the food industry. Also, it helps protect |
https://en.wikipedia.org/wiki/Pentalenene%20synthase | The enzyme pentalenene synthase (EC 4.2.3.7) catalyzes the chemical reaction
(2E,6E)-farnesyl diphosphate pentalenene + 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 (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, pentalenene-forming). This enzyme is also called pentalenene synthetase.
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phaseollidin%20hydratase | The enzyme phaseollidin hydratase () catalyzes the chemical reaction
phaseollidin hydrate phaseollidin + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is phaseollidin-hydrate hydro-lyase (phaseollidin-forming). This enzyme is also called phaseollidin-hydrate hydro-lyase.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphogluconate%20dehydratase | The enzyme phosphogluconate dehydratase () catalyzes the chemical reaction
6-phospho-D-gluconate 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 6-phospho-D-gluconate hydro-lyase (2-dehydro-3-deoxy-6-phospho-D-gluconate-forming). Other names in common use include 6-phosphogluconate dehydratase, 6-phosphogluconic dehydrase, gluconate-6-phosphate dehydratase, gluconate 6-phosphate dehydratase, 6-phosphogluconate dehydrase, and 6-phospho-Dgluconate hydro-lyase. This enzyme participates in the Entner–Doudoroff pathway.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Pinene%20synthase | In enzymology, a pinene synthase () is an enzyme that catalyzes the chemical reaction
geranyl diphosphate pinene + diphosphate
Hence, this enzyme has one substrate, geranyl diphosphate, and two products, pinene and 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 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 structure |
https://en.wikipedia.org/wiki/Poly%28alpha-L-guluronate%29%20lyase | The enzyme guluronate-specific alginate lyase (, formerly called poly(α-L-guluronate) lyase) catalyzes the following process:
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and α-L-uluronate at their reducing end.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is alginate α-L-guluronate—uronate lyase. Other names in common use include alginase II, guluronate lyase, L-guluronan lyase, L-guluronate lyase, poly-α-L-guluronate lyase, and polyguluronate-specific alginate lyase'''.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 4.2.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Mannuronate-specific%20alginate%20lyase | The enzyme mannuronate-specific alginate lyase (, formerly called poly(β-D-mannuronate) lyase) catalyzes the degradation of alginate into various monosaccharide and polysaccharide products:
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-α-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and β-D-mannuronate at their reducing end.
Alginate lyase cleaves the glycosidic bonds of alginate via a β-elimination mechanism, in which it first converts alginate into several oligosaccharides containing unsaturated uronic acids at their non-reducing ends. It then cleaves the oligosaccharides, forming 4-deosy-L-erythro-5-hexoseulose uronic acid.
This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is alginate β-D-mannuronate—uronate lyase. Other names in common use include alginate lyase I, alginate lyase, alginase I, alginase II, and alginase. This enzyme participates in fructose and mannose metabolism.
Substrate specificity
Alginate is a linear polysaccharide that has been isolated from a variety of organisms, ranging from viruses and bacteria to fungi. It is also a major component of the cell wall in brown algae and a major source of fixed carbon for other organisms. Many organisms from which alginate lyase has been isolated are found in close association with brown algae. For example, some strains of bacteria from the Paenibacillus genus were is |
https://en.wikipedia.org/wiki/Prephenate%20dehydratase | The enzyme prephenate dehydratase () catalyzes the chemical reaction
prephenate phenylpyruvate + H2O + CO2
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is prephenate hydro-lyase (decarboxylating; phenylpyruvate-forming). This enzyme is also called prephenate hydro-lyase (decarboxylating). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Propanediol%20dehydratase | The enzyme propanediol dehydratase () catalyzes the chemical reaction
propane-1,2-diol propanal + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is propane-1,2-diol hydro-lyase (propanal-forming). Other names in common use include meso-2,3-butanediol dehydrase, diol dehydratase, DL-1,2-propanediol hydro-lyase, diol dehydrase, adenosylcobalamin-dependent diol dehydratase, propanediol dehydrase, coenzyme B12-dependent diol dehydrase, 1,2-propanediol dehydratase, dioldehydratase, and propane-1,2-diol hydro-lyase. This enzyme participates in glycerolipid metabolism. It employs one cofactor, cobamide.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 4.2.1
Cobamide enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Suburbia%20%28department%20store%29 | Suburbia is a chain of department stores founded in 1970 in Mexico City. Its main activity consists of the sale of clothing, appliances, electronics and cell phones aimed at the socioeconomic middle and low classes. Suburbia currently has 166 stores in the Mexican Republic.
History
The first branch was opened on October 28, 1970, in Taxqueña, south of Mexico City, in which its concept was born as a department store for clothing, footwear and accessories for the whole family. In 1986, together with Aurrerá, Bodega Aurrerá, Superama, Vips and El Portón, Grupo Cifra was created. In 1994, together with Vips, Suburbia joined the Cifra Walmart group (which in turn changed to Walmart de México in 2001). In 1997, Suburbia had more than 9,000 employees.
On January 18, 2016, Walmart de México announced the start of the sales process for this format, which ended when the El Puerto de Liverpool chain acquired 100% of the chain on August 10, 2016. The final closure of the operation (purchase) was carried out on March 10, 2017, when the Federal Economic Competition Commission authorized the sale. On April 4, having concluded the formalities of the transaction, the incorporation of the same to Liverpool began.
On September 12, 2018, Grupo Liverpool announced that the format Fábricas de Francia will disappear to convert the 41 stores into the Liverpool or Suburbia formats. In 2019, while 70% of Fábricas de Francia stores moved to Liverpool, the remaining 21 branches became Suburbia store |
https://en.wikipedia.org/wiki/Protoaphin-aglucone%20dehydratase%20%28cyclizing%29 | The enzyme protoaphin-aglucone dehydratase (cyclizing) () catalyzes the chemical reaction
protoaphin aglucone xanthoaphin + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is protoaphin-aglucone hydro-lyase (cyclizing; xanthoaphin-forming). Other names in common use include protoaphin dehydratase, protoaphin dehydratase (cyclizing), and protoaphin-aglucone hydro-lyase (cyclizing).
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pseudouridylate%20synthase | The enzyme pseudouridylate synthase () catalyzes the chemical reaction
uracil + D-ribose 5-phosphate pseudouridine 5′-phosphate + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is uracil hydro-lyase (adding D-ribose 5-phosphate pseudouridine-5′-phosphate-forming). Other names in common use include pseudouridylic acid synthetase, pseudouridine monophosphate synthetase, 5-ribosyluracil 5-phosphate synthetase, pseudouridylate synthetase, upsilonUMP synthetase, and uracil hydro-lyase (adding D-ribose 5-phosphate). This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, 22 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , and .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Pyrazolylalanine%20synthase | The enzyme pyrazolylalanine synthase () catalyzes the chemical reaction
L-serine + pyrazole 3-(pyrazol-1-yl)-L-alanine + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-serine hydro-lyase [adding pyrazole 3-(pyrazol-1-yl)-L-alanine-forming]. Other names in common use include β-pyrazolylalaninase, β-(1-pyrazolyl)alanine synthase, and L-serine hydro-lyase (adding pyrazole). It employs one cofactor, pyridoxal phosphate.
References
EC 4.2.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-2-methylmalate%20dehydratase | The enzyme(R)-2-methylmalate dehydratase () catalyzes the chemical reaction
(R)-2-methylmalate 2-methylmaleate + HO
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is {{chem name|(R)-2-methylmalate hydro-lyase (2-methylmaleate-forming)}}. Other names in common use include , and . This enzyme participates in valine, leucine and isoleucine biosynthesis and c5-branched dibasic acid metabolism. It employs one cofactor, iron.
References
EC 4.2.1
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28R%29-limonene%20synthase | The enzyme (R)-limonene synthase (EC 4.2.3.20) catalyzes the reversible chemical reaction
geranyl diphosphate (+)-(4R)-limonene + 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 geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-(4R)-limonene-forming]. Other names in common use include (+)-limonene synthase, and geranyldiphosphate diphosphate lyase [(+)-(R)-limonene-forming]. This enzyme participates in monoterpenoid biosynthesis and is localized to Leucoplasts of oil gland secretory cells.
References
Further reading
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/R-linalool%20synthase | The enzyme R-linalool synthase (EC 4.2.3.26) catalyzes the chemical reaction
geranyl diphosphate + H2O (3R)-linalool + 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 geranyl-diphosphate diphosphate-lyase [(3R)-linalool-forming]. Other names in common use include (3R)-linalool synthase, and (−)-3R-linalool synthase.
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-2-methylmalate%20dehydratase | The enzyme (S)-2-methylmalate dehydratase () catalyzes the chemical reaction:
(S)-2-methylmalate 2-methylfumarate + HO
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is
(S)-2-methylmalate hydro-lyase (2-methylfumarate-forming). Other names in common use include mesaconate hydratase, (+)-citramalate hydro-lyase, L-citramalate hydrolase, citramalate dehydratase, (+)-citramalic hydro-lyase, mesaconate mesaconase, mesaconase, and (S)-2-methylmalate hydro-lyase.
This enzyme participates in c5-branched dibasic acid metabolism. In addition, the family of lyases which is also an enzyme catalyzes the breaking the elimination reaction of the variety of amounts of chemical bonds from hydrolysis (a substitution reaction ) and oxidation, which forms a new double bond or a new ring structure.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/KAT2A |
Histone acetyltransferase KAT2A is an enzyme that in humans is encoded by the KAT2A gene.
Interactions
GCN5L2 has been shown to interact with:
DDB1,
Ku70,
Ku80,
TADA2L,
TAF9, and
Transcription initiation protein SPT3 homolog.
References
Further reading
External links |
https://en.wikipedia.org/wiki/Sabinene-hydrate%20synthase | The enzyme sabinene-hydrate synthase (EC 4.2.3.11) catalyzes the chemical reaction
geranyl diphosphate + H2O sabinene hydrate + 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 geranyl-diphosphate diphosphate-lyase (cyclizing, sabinene-hydrate-forming). This enzyme is also called sabinene hydrate cyclase. This enzyme participates in monoterpenoid biosynthesis.
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Scytalone%20dehydratase | The enzyme scytalone dehydratase () catalyzes the chemical reaction
scytalone 1,3,8-trihydroxynaphthalene + H2O
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is scytalone 7,8-hydro-lyase (1,3,8-trihydroxynaphthalene-forming). This enzyme is also called scytalone 7,8-hydro-lyase.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 4.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/S-linalool%20synthase | The enzyme S-linalool synthase (EC 4.2.3.25) catalyzes the chemical reaction
geranyl diphosphate + H2O (3S)-linalool + 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 geranyl-diphosphate diphosphate-lyase [(3S)-linalool-forming]. Other names in common use include LIS, Lis, and 3S-linalool synthase.
References
EC 4.2.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-norcoclaurine%20synthase | The enzyme (S)-norcoclaurine synthase () catalyzes the chemical reaction
4-hydroxyphenylacetaldehyde + 4-(2-aminoethyl)benzene-1,2-diol (Dopamine) (S)-norcoclaurine + HO
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 4-hydroxyphenylacetaldehyde hydro-lyase [adding dopamine (S)-norcoclaurine-forming]. Other names in common use include (S)-norlaudanosoline synthase, and 4-hydroxyphenylacetaldehyde hydro-lyase (adding dopamine). This enzyme participates in benzylisoquinoline alkaloid biosynthesis.
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Synephrine%20dehydratase | The enzyme synephrine dehydratase () catalyzes the chemical reaction
(R)-synephrine (4-hydroxyphenyl)acetaldehyde + methylamine
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (R)-synephrine hydro-lyase (methylamine-forming).
References
EC 4.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Taxadiene%20synthase | The enzyme taxadiene synthase (EC 4.2.3.17) catalyzes the chemical reaction
geranylgeranyl diphosphate taxa-4,11-diene + 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 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 |
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