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intramolecular lyases - metabolism (342) 342
intramolecular lyases - genetics (324) 324
index medicus (310) 310
biochemistry & molecular biology (288) 288
molecular sequence data (250) 250
amino acid sequence (214) 214
enzymes (200) 200
biosynthesis (198) 198
plant sciences (188) 188
plants (131) 131
base sequence (124) 124
physiological aspects (123) 123
research (123) 123
intramolecular lyases (119) 119
intramolecular transferases - metabolism (118) 118
plant proteins - metabolism (115) 115
escherichia-coli (113) 113
cloning, molecular (112) 112
intramolecular lyases - chemistry (112) 112
expression (111) 111
substrate specificity (109) 109
gene expression regulation, plant (106) 106
analysis (105) 105
kinetics (99) 99
plant proteins - genetics (99) 99
gene expression (94) 94
escherichia coli - genetics (92) 92
sequence homology, amino acid (90) 90
mutation (87) 87
microbiology (85) 85
isomerases - metabolism (83) 83
phylogeny (83) 83
genes (82) 82
catalysis (81) 81
carotenoids - biosynthesis (75) 75
cloning (71) 71
carotenoids - metabolism (70) 70
models, molecular (70) 70
terpenes - metabolism (69) 69
proteins (66) 66
biophysics (65) 65
cell biology (62) 62
sequence alignment (62) 62
biotechnology & applied microbiology (61) 61
intramolecular transferases - genetics (61) 61
lycopene (60) 60
metabolism (60) 60
animals (59) 59
intramolecular oxidoreductases - metabolism (59) 59
carotenoids (57) 57
genetic aspects (57) 57
food and beverages (56) 56
plants, genetically modified (56) 56
recombinant proteins - metabolism (56) 56
arabidopsis - genetics (55) 55
bacterial proteins - metabolism (55) 55
research article (55) 55
binding sites (54) 54
intramolecular transferases - chemistry (53) 53
life sciences (53) 53
arabidopsis (52) 52
crystal-structure (51) 51
sequence analysis, dna (51) 51
multidisciplinary sciences (50) 50
bacterial proteins - genetics (49) 49
arabidopsis-thaliana (47) 47
beta-carotene (47) 47
mechanism (47) 47
molecular structure (47) 47
escherichia coli - enzymology (46) 46
escherichia coli - metabolism (45) 45
oxidoreductases - genetics (45) 45
stereoisomerism (45) 45
carotenoid biosynthesis (44) 44
genes, plant (44) 44
isomerases - genetics (44) 44
oxidoreductases - metabolism (44) 44
identification (43) 43
monoterpenes (43) 43
arabidopsis - enzymology (42) 42
gene (42) 42
gene expression regulation, enzymologic (42) 42
pathway (42) 42
plants - enzymology (42) 42
article (41) 41
protein conformation (41) 41
purification (41) 41
alkyl and aryl transferases - genetics (40) 40
bacteria (40) 40
chromatography, high pressure liquid (40) 40
intramolecular oxidoreductases - genetics (40) 40
molecular-cloning (40) 40
crystallography, x-ray (39) 39
flavonoids (39) 39
chemical properties (38) 38
cytochrome p-450 enzyme system - metabolism (38) 38
gene-expression (38) 38
humans (38) 38
recombinant proteins - genetics (38) 38
alkyl and aryl transferases - metabolism (37) 37
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1. Full Text Ammonia lyases and aminomutases as biocatalysts for the synthesis of α-amino and β-amino acids
by Turner, Nicholas J
Current Opinion in Chemical Biology, ISSN 1367-5931, 04/2011, Volume 15, Issue 2, pp. 234 - 240
Ammonia lyases catalyse the reversible addition of ammonia to cinnamic acid ( : R = H) and -hydroxycinnamic ( : R = OH) to generate -phenylalanine ( : R = H)... 
RHODOTORULA-GLUTINIS | BIOPHYSICS | MECHANISM | PROMISCUITY | CRYSTAL-STRUCTURE | ENZYMES | BIOCHEMISTRY & MOLECULAR BIOLOGY | CINNAMIC ACID | TYROSINE AMINOMUTASE | L-PHENYLALANINE | DISCOVERY | Bacteria - metabolism | Biocatalysis | Ammonia - metabolism | Humans | Amino Acids - chemistry | Ammonia-Lyases - metabolism | Isomerism | Intramolecular Transferases - metabolism | Amino Acids - metabolism | Biotechnology - methods | Animals | Bacteria - enzymology | Bacterial Proteins - metabolism
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2. Full Text Structural and Chemical Biology of Terpenoid Cyclases
by Christianson, David W
Chemical Reviews, ISSN 0009-2665, 09/2017, Volume 117, Issue 17, pp. 11570 - 11648
The year 2017 marks the twentieth anniversary of terpenoid cyclase structural biology: a trio of terpenoid cyclase structures reported together in 1997 were... 
OCTAPRENYL PYROPHOSPHATE SYNTHASE | STREPTOMYCES-COELICOLOR A3 | BIFUNCTIONAL ABIETADIENE SYNTHASE | FARNESYL-DIPHOSPHATE SYNTHASE | PRODUCT CHAIN-LENGTH | TOBACCO 5-EPI-ARISTOLOCHENE SYNTHASE | SESQUITERPENE ANTIBIOTIC ALBAFLAVENONE | FIR ABIES-GRANDIS | SITE-DIRECTED MUTAGENESIS | CHEMISTRY, MULTIDISCIPLINARY | SQUALENE-HOPENE CYCLASES | Protein Structure, Tertiary | Alkyl and Aryl Transferases - chemistry | Terpenes - chemistry | Terpenes - metabolism | Intramolecular Lyases - metabolism | Alkyl and Aryl Transferases - metabolism | Dimethylallyltranstransferase - metabolism | Crystallography, X-Ray | Carbon-Carbon Lyases - chemistry | Carbon-Carbon Lyases - metabolism | Intramolecular Lyases - chemistry | Dimethylallyltranstransferase - chemistry | Review
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3. Full Text Synthetic and therapeutic applications of ammonia-lyases and aminomutases
by Parmeggiani, Fabio and Weise, Nicholas J and Ahmed, Syed T and Turner, Nicholas J
Chemical Reviews, ISSN 0009-2665, 2018, Volume 118, Issue 1, pp. 73 - 118
Ammonia-lyases and aminomutases are mechanistically and structurally diverse enzymes which catalyze the deamination and/or isomerization of amino acids in... 
BETA-AMINO ACIDS | GREEN FLUORESCENT PROTEIN | BIOSYNTHETIC GENE-CLUSTER | BROAD SUBSTRATE-SPECIFICITY | 4-METHYLIDENEIMIDAZOLE-5-ONE-CONTAINING TYROSINE AMINOMUTASE | ISLANDICUS PENICILLIUM-ISLANDICUM | RADICAL SAM SUPERFAMILY | L-ASPARTIC ACID | ANTIBIOTIC C-1027 BIOSYNTHESIS | SITE-DIRECTED MUTAGENESIS | CHEMISTRY, MULTIDISCIPLINARY | Phenylalanine Ammonia-Lyase - classification | Biocatalysis | Humans | Models, Molecular | Substrate Specificity | Ammonia-Lyases - metabolism | Transaminases - classification | Phenylalanine Ammonia-Lyase - chemistry | Phenylalanine Ammonia-Lyase - metabolism | Intramolecular Transferases - metabolism | Ammonia-Lyases - therapeutic use | Ammonia-Lyases - classification | Transaminases - metabolism | Bacteria - enzymology | Intramolecular Transferases - therapeutic use | Transaminases - therapeutic use | Intramolecular Transferases - classification
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4. Full Text Double function hydroperoxide lyases/epoxyalcohol synthases (CYP74C) of higher plants: identification and conversion into allene oxide synthases by site-directed mutagenesis
by Toporkova, Yana Y and Gorina, Svetlana S and Bessolitsyna, Elena K and Smirnova, Elena O and Fatykhova, Valeria S and Brühlmann, Fredi and Ilyina, Tatiana M and Mukhtarova, Lucia S and Grechkin, Alexander N
BBA - Molecular and Cell Biology of Lipids, ISSN 1388-1981, 04/2018, Volume 1863, Issue 4, pp. 369 - 378
The CYP74C subfamily of fatty acid hydroperoxide transforming enzymes includes hydroperoxide lyases (HPLs) and allene oxide synthases (AOSs). This work reports... 
Epoxyalcohol synthase | CYP74C subfamily enzymes | Hydroperoxide lyase | Cytochrome P450 | Site-directed mutagenesis | Oxylipins | CYSTEINE.FECL3 CATALYST | OXYLIPIN BIOSYNTHESIS | LINOLEIC-ACID | BIOCHEMISTRY & MOLECULAR BIOLOGY | FATTY-ACID HYDROPEROXIDES | DIVINYL ETHER SYNTHASES | SIMILAR BIOCHEMICAL REACTIONS | CELL BIOLOGY | LIPOXYGENASE PATHWAY | BIOPHYSICS | MOLECULAR-CLONING | LYASE | Aldehyde-Lyases - chemistry | Amino Acid Sequence | Biocatalysis | Gas Chromatography-Mass Spectrometry | Mutagenesis, Site-Directed | Cytochrome P-450 Enzyme System - metabolism | Substrate Specificity | Mutant Proteins - metabolism | Lipid Peroxides - metabolism | Phylogeny | Linoleic Acids - metabolism | Linolenic Acids - metabolism | Plants - enzymology | Recombinant Proteins - isolation & purification | Cytochrome P-450 Enzyme System - chemistry | Sequence Alignment | Linolenic Acids - chemistry | Lipid Peroxides - chemistry | Aldehyde-Lyases - metabolism | Plant Proteins - metabolism | Kinetics | Intramolecular Oxidoreductases - metabolism | Linoleic Acids - chemistry | Enzymes | Unsaturated fatty acids | Plants | Glycine | Epoxy resins | Index Medicus
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5. Full Text Aspartase/Fumarase Superfamily: A Common Catalytic Strategy Involving General Base-Catalyzed Formation of a Highly Stabilized aci-Carboxylate Intermediate
by Veetil, Vinod Puthan and Fibriansah, Guntur and Raj, Hans and Thunnissen, Andy-Mark W. H and Poelarends, Gerrit J
Biochemistry, ISSN 0006-2960, 05/2012, Volume 51, Issue 21, pp. 4237 - 4243
Members of the aspartase/fumarase superfamily share a common tertiary and quaternary fold, as well as a similar active site architecture; the superfamily... 
CHEMICAL MECHANISM | ACTIVE-SITE | ARGININOSUCCINATE LYASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | 3-CARBOXY-CIS,CIS-MUCONATE LACTONIZING ENZYME | BACILLUS SP YM55-1 | ASPARTATE AMMONIA-LYASE | SUBTILIS ADENYLOSUCCINATE LYASE | SITE-DIRECTED MUTAGENESIS | Argininosuccinate Lyase - chemistry | Intramolecular Lyases - metabolism | Saccharomyces cerevisiae - genetics | Humans | Aspartate Ammonia-Lyase - chemistry | Fumarate Hydratase - chemistry | delta-Crystallins - metabolism | Molecular Sequence Data | Substrate Specificity | delta-Crystallins - genetics | Aspartate Ammonia-Lyase - metabolism | Argininosuccinate Lyase - metabolism | Aspartate Ammonia-Lyase - genetics | Adenylosuccinate Lyase - chemistry | Fumarate Hydratase - metabolism | Protein Structure, Quaternary | Conserved Sequence | Adenylosuccinate Lyase - genetics | Catalysis | Protein Structure, Tertiary | Amino Acid Sequence | Catalytic Domain | Argininosuccinate Lyase - genetics | Escherichia coli - enzymology | Models, Molecular | Escherichia coli Proteins - metabolism | Fumarate Hydratase - genetics | Saccharomyces cerevisiae Proteins - genetics | Sequence Homology, Amino Acid | delta-Crystallins - chemistry | Intramolecular Lyases - genetics | Escherichia coli - genetics | Saccharomyces cerevisiae Proteins - metabolism | Escherichia coli Proteins - genetics | Saccharomyces cerevisiae - enzymology | Adenylosuccinate Lyase - metabolism | Escherichia coli Proteins - chemistry | Intramolecular Lyases - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Enzyme binding | Fumarase | Chemical properties | Structure | Analysis
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6. Full Text Structural and functional insights into the reaction specificity of catalase-related hydroperoxide lyase: A shift from lyase activity to allene oxide synthase by site-directed mutagenesis
by Teder, Tarvi and Lõhelaid, Helike and Samel, Nigulas
PLoS ONE, ISSN 1932-6203, 09/2017, Volume 12, Issue 9, pp. e0185291 - e0185291
Two highly identical fusion proteins, an allene oxide synthase-lipoxygenase (AOS-LOX) and a hydroperoxide lyase-lipoxygenase (HPL-LOX), were identified in the... 
LIPOXYGENASE FUSION PROTEIN | PEROXIDASE | ACID | CORAL | METABOLISM | PATHWAY | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | MUTATION | CATALYTIC-ACTIVITY | IDENTIFICATION | Aldehyde-Lyases - chemistry | Amino Acid Sequence | Intramolecular Oxidoreductases - chemistry | Aldehyde-Lyases - isolation & purification | Electrophoresis, Polyacrylamide Gel | Protein Multimerization | Anthozoa - enzymology | Cytochrome P-450 Enzyme System - metabolism | Substrate Specificity | Mutagenesis, Site-Directed - methods | Mutant Proteins - metabolism | Cytochrome P-450 Enzyme System - isolation & purification | Hydrogen Peroxide - metabolism | Catalase - metabolism | Leukotrienes - chemistry | Leukotrienes - metabolism | Cytochrome P-450 Enzyme System - chemistry | Animals | Mutant Proteins - chemistry | Aldehyde-Lyases - metabolism | Ligands | Molecular Docking Simulation | Kinetics | Intramolecular Oxidoreductases - metabolism | Usage | Mutagenesis | Physiological aspects | Genetic aspects | Research | Lipase | Methods | Cytochrome | Residues | Hydroperoxide lyase | Amino acids | Biochemistry | Hydrophobicity | Arachidonic acid | Proteins | E coli | Catalase | Heme | Docking | Catalysis | Active control | Enzymes | Gene expression | Fatty acids | Chemistry | Acids | Allene | Liquid oxygen | Site-directed mutagenesis | Mutation | Lipoxygenase | Structural analysis | Structure-function relationships | Index Medicus
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7. Full Text Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis
by Ngaki, Micheline N and Louie, Gordon V and Philippe, Ryan N and Manning, Gerard and Pojer, Florence and Bowman, Marianne E and Li, Ling and Larsen, Elise and Wurtele, Eve Syrkin and Noel, Joseph P
Nature, ISSN 0028-0836, 05/2012, Volume 485, Issue 7399, pp. 530 - 533
Specialized metabolic enzymes biosynthesize chemicals of ecological importance, often sharing a pedigree with primary metabolic enzymes(1). However, the... 
TRANSFORMATION | PLANT | ARABIDOPSIS-THALIANA | GENE | TEMPERATURE | REACTION-MECHANISM | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | DIFFRACTION DATA | IDENTIFICATION | FUNCTIONAL GENOMICS | Arabidopsis - enzymology | Arabidopsis - growth & development | Intramolecular Lyases - metabolism | Stereoisomerism | Crystallography, X-Ray | Fatty Acid-Binding Proteins - metabolism | Intramolecular Lyases - deficiency | Arabidopsis Proteins - metabolism | Fatty Acid-Binding Proteins - deficiency | Fatty Acids - metabolism | Arabidopsis Proteins - genetics | Arabidopsis - chemistry | Biocatalysis | Models, Molecular | Fatty Acid-Binding Proteins - genetics | Protein Folding | Arabidopsis - genetics | Phenotype | Arabidopsis Proteins - chemistry | Intramolecular Lyases - genetics | alpha-Linolenic Acid - metabolism | Protein Binding | Fatty Acid-Binding Proteins - chemistry | Ligands | Intramolecular Lyases - chemistry | Evolution, Molecular | Physiological aspects | Isomerases | Research | Arabidopsis | Fatty acids | Protein binding | Proteins | Enzymes | Flowers & plants
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8. Full Text Understanding Which Residues of the Active Site and Loop Structure of a Tyrosine Aminomutase Define Its Mutase and Lyase Activities
by Attanayake, Gayanthi and Walter, Tyler and Walker, Kevin D
Biochemistry, ISSN 0006-2960, 06/2018, Volume 57, Issue 25, pp. 3503 - 3514
Site-directed mutations and substrate analogues were used to gain insights into the branch-point reaction of the 3,5-dihydro-5-methylidene-4H-imidazol-4-one... 
SUBSTRATE-SPECIFICITY | MECHANISM | DETERMINANTS | AMINO-ACIDS | RETENTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | STEREOCHEMISTRY | CONFIGURATION | ANTIBIOTIC C-1027 BIOSYNTHESIS | PHENYLALANINE AMMONIA-LYASE | MUTATIONAL ANALYSIS | Amino Acid Sequence | Catalytic Domain | Phenylalanine - metabolism | Oryza - metabolism | Stereoisomerism | Models, Molecular | Substrate Specificity | Oryza - chemistry | Lyases - metabolism | Oryza - enzymology | Intramolecular Transferases - metabolism | Sequence Alignment | Tyrosine - metabolism | Phenylalanine - chemistry | Plant Proteins - chemistry | Lyases - chemistry | Protein Conformation | Plant Proteins - metabolism | Intramolecular Transferases - chemistry | Tyrosine - chemistry
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9. Full Text The hydroperoxide lyase branch of the oxylipin pathway protects against photoinhibition of photosynthesis
by Savchenko, Tatyana and Yanykin, Denis and Khorobrykh, Andrew and Terentyev, Vasily and Klimov, Vyacheslav and Dehesh, Katayoon
Planta, ISSN 0032-0935, 06/2017, Volume 245, Issue 6, pp. 1179 - 1192
Main conclusion This study describes a new role for hydroperoxide lyase branch of oxylipin biosynthesis pathway in protecting photosynthetic apparatus under... 
Photoinhibition | Photosystem 2 | Hydroperoxide lyase | High light stress | Allene oxide synthase | Oxylipins | 12-OXO-PHYTODIENOIC ACID | ARABIDOPSIS-THALIANA | CHLOROPHYLL FLUORESCENCE | LINOLENIC ACID | PLANT SCIENCES | METHYL JASMONATE | NICOTIANA-ATTENUATA | GENE-EXPRESSION | JASMONIC ACID | VOLATILE ORGANIC-COMPOUNDS | Acetates - metabolism | Cytochrome P-450 Enzyme System - metabolism | Thylakoids - metabolism | Arabidopsis - metabolism | Photosystem II Protein Complex - metabolism | Oxylipins - metabolism | Photosynthesis - genetics | Light | Photosynthesis - physiology | alpha-Linolenic Acid - metabolism | Aldehyde-Lyases - metabolism | Cyclopentanes - metabolism | Intramolecular Oxidoreductases - metabolism | Arabidopsis thaliana | Chlorophyll | Metabolites | Analysis | Phytochemistry | Linolenic acids | Photosynthesis | Competition | Regulations | Membranes | Photosynthetic apparatus | Adaptability | Fluorescence | Lipids | Data processing | Biosynthesis | Plants | Methyl jasmonate | Thylakoid membranes | Leaves | Photosystem | Linolenic acid | Acids | Presenilin 2 | Jasmonic acid | Genotypes
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10. Full Text Cooperative functioning between phenylalanine ammonia lyase and isochorismate synthase activities contributes to salicylic acid biosynthesis in soybean
by Shine, M. B and Yang, Jung‐Wook and El‐Habbak, Mohamed and Nagyabhyru, Padmaja and Fu, Da‐Qi and Navarre, Duroy and Ghabrial, Said and Kachroo, Pradeep and Kachroo, Aardra
New Phytologist, ISSN 0028-646X, 11/2016, Volume 212, Issue 3, pp. 627 - 636
Salicylic acid ( SA ), an essential regulator of plant defense, is derived from chorismate via either the phenylalanine ammonia lyase ( PAL ) or the... 
soybean | pathogen defense | isochorismate synthase | ICS | phenylalanine ammonia lyase | PAL | salicylic acid | Glycine max | salicylic acid (SA) | isochorismate synthase (ICS) | phenylalanine ammonia lyase (PAL) | soybean (Glycine max) | PHYTOPHTHORA RESISTANCE | BENZOIC-ACID | PSEUDOMONAS-SYRINGAE | SYSTEMIC ACQUIRED-RESISTANCE | PLANT SCIENCES | PERONOSPORA-PARASITICA | AMINO-ACID | SYRINGAE PV GLYCINEA | PLANT DEFENSE | RACE-SPECIFIC RESISTANCE | AVIRULENCE GENE | Intramolecular Transferases - genetics | Genes, Plant | Salicylic Acid - metabolism | RNA, Messenger - genetics | Gene Silencing | Phytophthora - physiology | Biosynthetic Pathways | RNA, Messenger - metabolism | Soybeans - genetics | Phenylalanine Ammonia-Lyase - metabolism | Intramolecular Transferases - metabolism | Plant Proteins - genetics | Phenylalanine Ammonia-Lyase - genetics | Plant Leaves - metabolism | Isoenzymes - metabolism | Soybeans - enzymology | Soybeans - microbiology | Gene Expression Regulation, Plant | Plant Proteins - metabolism | Plant Diseases | Disease Resistance - genetics | Pseudomonas syringae - physiology | Proteins | Arabidopsis thaliana | Ammonia | Drug resistance in microorganisms | Phenylalanine | Analysis | Physiological aspects | Phenols | Virulence (Microbiology) | Soybean | Glycine | Gene expression
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11. Full Text Natural Genetic Variation in Lycopene Epsilon Cyclase Tapped for Maize Biofortification
by Carlos E. Harjes and Torbert R. Rocheford and Ling Bai and Thomas P. Brutnell and Catherine Bermudez Kandianis and Stephen G. Sowinski and Ann E. Stapleton and Ratnakar Vallabhaneni and Mark Williams and Eleanore T. Wurtzel and Jianbing Yan and Edward S. Buckler
Science, ISSN 0036-8075, 1/2008, Volume 319, Issue 5861, pp. 330 - 333
Dietary vitamin A deficiency causes eye disease in 40 million children each year and places 140 to 250 million at risk for health disorders. Many children in... 
Quantitative trait loci | Haplotypes | Vitamin A | Carotenoids | Colors | Breeding | Genetic variation | Corn | Inbreeding | Genetic loci | Reports | Y1 GENE | LINKAGE DISEQUILIBRIUM | VITAMIN-A-DEFICIENCY | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | CAROTENOIDS | PLANTS | PHYTOENE SYNTHASE | FORTIFICATION | REVEALS | Zea mays - chemistry | Zea mays - genetics | Carotenoids - analysis | Intramolecular Lyases - metabolism | Nutritive Value | Zea mays - enzymology | Molecular Sequence Data | Xanthophylls - analysis | beta Carotene - metabolism | Polymorphism, Genetic | Genetic Variation | Intramolecular Lyases - genetics | Mutagenesis | Base Sequence | Carotenoids - metabolism | Gene Expression Regulation, Plant | Xanthophylls - metabolism | Cryptoxanthins | Quantitative Trait Loci | beta Carotene - analysis | Crosses, Genetic | Genetic engineering | Malnutrition | Transgenic plants | Index Medicus
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12. Full Text Twin anchors of the soybean isoflavonoid metabolon: evidence for tethering of the complex to the endoplasmic reticulum by IFS and C4H
by Dastmalchi, Mehran and Bernards, Mark A and Dhaubhadel, Sangeeta
The Plant Journal, ISSN 0960-7412, 03/2016, Volume 85, Issue 6, pp. 689 - 706
Isoflavonoids are specialized plant metabolites, almost exclusive to legumes, and their biosynthesis forms a branch of the diverse phenylpropanoid pathway.... 
soybean | protein–protein interaction | specialized metabolism | metabolon | isoflavonoids | isoform specificity | protein-protein interaction | ARABIDOPSIS-THALIANA | FLAVONOID ENZYMES | SUBCELLULAR-LOCALIZATION | PLANT-CELLS | ENTRY POINT | PLANT SCIENCES | PHENYLPROPANOID PATHWAY | BRADYRHIZOBIUM-JAPONICUM | PROTEIN-PROTEIN INTERACTIONS | FUSARIUM-SOLANI | L-PHENYLALANINE | Plant Roots - metabolism | Intramolecular Lyases - metabolism | Cytochrome P-450 Enzyme System - metabolism | Endoplasmic Reticulum - metabolism | Trans-Cinnamate 4-Monooxygenase - genetics | Alcohol Oxidoreductases - metabolism | Cytoplasm - metabolism | Isoflavones - metabolism | Soybeans - genetics | Soybeans - metabolism | Alcohol Oxidoreductases - genetics | Plant Proteins - genetics | Protein Interaction Mapping - methods | Trans-Cinnamate 4-Monooxygenase - metabolism | Intramolecular Lyases - genetics | Oxygenases - metabolism | Plants, Genetically Modified | Protein Isoforms | Plant Proteins - metabolism | Oxygenases - genetics | Soybean | Cytochrome | Enzymes | Soybeans | Biosynthesis | Metabolites | Endoplasmic reticulum
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13. Full Text Manipulation of Phytoene Levels in Tomato Fruit: Effects on Isoprenoids, Plastids, and Intermediary Metabolism
by Paul D. Fraser and Eugenia M. A. Enfissi and John M. Halket and Mark R. Truesdale and Dongmei Yu and Christopher Gerrish and Peter M. Bramley
The Plant Cell, ISSN 1040-4651, 10/2007, Volume 19, Issue 10, pp. 3194 - 3211
In tomato (Solanum lycopersicum), phytoene synthase-1 (PSY-1) is the key biosynthetic enzyme responsible for the synthesis of fruit carotenoids. To further our... 
Ripening | Carotenoids | Fruiting | Amino acids | Plants | Plastids | Transgenic plants | Fatty acids | Chlorophylls | Fruits | ELUCIDATION | METHYLERYTHRITOL PHOSPHATE-PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLANT SCIENCES | CELL BIOLOGY | LYCOPENE ACCUMULATION | SYNTHASE | BETA-CAROTENE | CLONING | BIOSYNTHESIS | PLANTS | ARABIDOPSIS | REVEALS | Gas Chromatography-Mass Spectrometry | Intramolecular Lyases - metabolism | Alkyl and Aryl Transferases - metabolism | Lycopersicon esculentum - growth & development | Seeds - growth & development | Alkyl and Aryl Transferases - genetics | Germination - genetics | Plants, Genetically Modified | Gene Expression Regulation, Plant | Polymerase Chain Reaction | Geranylgeranyl-Diphosphate Geranylgeranyltransferase | Plastids - genetics | Lycopersicon esculentum - genetics | Plastids - metabolism | Plant Proteins - metabolism | Fruit - metabolism | Fruit - genetics | Lycopersicon esculentum - metabolism | Seeds - metabolism | Seeds - genetics | beta Carotene - metabolism | Fruit - growth & development | Plant Proteins - genetics | Intramolecular Lyases - genetics | Models, Biological | Carotenoids - metabolism | Enzymes | Phytochemistry | Physiological aspects | Development | Genetic aspects | Research | Tomatoes | Chemical properties
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