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malfunction
HMG-CoA synthase 1 knockdown causes a compensating increase in HMG-CoA lyase protein level because of attenuated protein degradation
evolution
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a total of 53 3-hydroxy-3-methylglutaryl coenzyme A synthase genes in 23 land plant species, while no 3-hydroxy-3-methylglutaryl coenzyme A synthase genes are detected in three green algae species. The phylogenetic analysis suggests that plant 3-hydroxy-3-methylglutaryl coenzyme A synthase genes may have originated from a common ancestral gene before clustering in different branches during the divergence of plant lineages. Six 3-hydroxy-3-methylglutaryl coenzyme A synthase genes are detected in the allotetraploid cotton species (Gossypium hirsutum), which was twice that of the two diploid cotton species (Gossypium raimondii and Gossypium arboreum). The comparison of gene structures and phylogenetic analysis of 3-hydroxy-3-methylglutaryl coenzyme A synthase genes reveales conserved evolution during polyploidization in Gossypium. The sequence and expression divergence of duplicated genes in Gossypium hirsutum implied the sub-functionalization of GhHMGS1A and GhHMGS1D as well as GhHMGS3A and GhHMGS3D, whereas it implied the pseudogenization of GhHMGS2A and GhHMGS2D. The study unravels the evolutionary history of 3-hydroxy-3-methylglutaryl coenzyme A synthase genes in green plants and from diploid to allotetraploid in cotton and illustrates the different evolutionary fates of duplicated 3-hydroxy-3-methylglutaryl coenzyme A synthase genes resulting from polyploidization
evolution
the evolutionarily conserved nature of some single nucleotide polymorphisms is identified by comparative DNA sequence analysis of hydroxy-methylglutaryl coenzyme-A synthase orthologues from diverse taxa, demonstrating the molecular evolution of rubber biosynthesis genes in general
evolution
the sequence of the 3-hydroxy-3-methylglutaryl coenzyme A synthase from Chamaemelum nobile is highly homologous to those of HMGS proteins from other plant species. Phylogenetic tree analysis reveals that CnHMGS clusters with the 3-hydroxy-3-methylglutaryl coenzyme A synthase of asteraceae in the dicotyledon clade
metabolism
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3-hydroxy-3-methylglutaryl-CoA synthase is the second enzyme in the cytosolic mevalonate pathway
metabolism
first committed enzyme in the mevalonate pathway. The enzyme plays an important role in the biosynthesis of the sesquiterpene, which is the main constituent of essential oil in Matricaria chamomilla
metabolism
in myxobacteria, the enzyme is involved in an alternative and acetyl-CoA-dependent isovaleryl CoA biosynthesis pathway
metabolism
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key enzyme in the mevalonate pathway
metabolism
overexpression of 3-hydroxy-3-methylglutaryl-coenzyme A synthase increases the production of monoterpenes and sesquiterpenes. The enzyme could play an important role in the yield of monoterpenes and sesquiterpenes
metabolism
overexpression of Brassica juncea wild-type and mutant (S359A) 3-hydroxy-3-methylglutaryl-coenzyme A synthase in Solanum lycopersicum, causes an accumulation of mevalonate-derived squalene and phytosterols, as well as methylerythritol phosphate (methylerythritol phosphate)-derived alpha-tocopherol (vitamin E) and carotenoids. Genes associated with the biosyntheses of C10, C15 and C20 universal precursors of isoprenoids, phytosterols, brassino-steroids, dolichols, methylerythritol phosphate, carotenoid and vitamin E are upregulated. In S359A tomato fruits, increased squalene and phytosterol contents over wild-type fruits are attributed to heightened SlHMGR2, SlFPS1, SlSQS and SlCYP710A11 expression. In both tomato wild-type and S359A fruits, the up-regulation of SlGPS and SlGGPPS1 in the mevalonate pathway that leads to alpha-tocopherol and carotenoid accumulation indicates cross-talk between the mevalonate and methylerythritol phosphate pathways. The manipulation of Brassica juncea 3-hydroxy-3-methylglutaryl-coenzyme A synthase 1 (HMGS1) represents a promising strategy to simultaneously elevate health-promoting squalene, phytosterols, alpha-tocopherol and carotenoids in tomato, an edible fruit
metabolism
rate-limiting enzyme in the cytoplasmic isoprenoid biosynthesis pathway leading to natural rubber production in Hevea brasiliensis
metabolism
the enzyme catalyses a step of the mevalonate pathway. Overexpression of HMG-CoA synthase promotes Arabidopsis root growth and inhibits glucosinolate biosynthesis, due to down-regulation of glucosinolate biosynthesis-related genes, up-regulation of sterol biosynthesis-related genes, and increase in sterol content
metabolism
the enzyme catalyze the crucial step in the mevalonate pathway in plants
metabolism
the enzyme catalyzes a reaction in the mevalonate pathway. Mevalonate is a building block of archaeal lipids. Three enzymes are involved in its biosynthesis: acetoacetyl-CoA thiolase (thiolase), 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGCS), and HMG-CoA reductase. The thiolase reaction is highly endergonic. In the thiolase/HMGCS complex, the endergonic thiolase reaction is directly coupled to the exergonic 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase reaction. A third protein spatially connects both enzymes. The two enzymes share the same substrate-binding site. Genomic information indicates that the presence of a thiolase/HMGCS complex is common in most of archaea and many bacteria
metabolism
the enzyme is implicated in latex metabolism
metabolism
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in myxobacteria, the enzyme is involved in an alternative and acetyl-CoA-dependent isovaleryl CoA biosynthesis pathway
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metabolism
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the enzyme catalyzes a reaction in the mevalonate pathway. Mevalonate is a building block of archaeal lipids. Three enzymes are involved in its biosynthesis: acetoacetyl-CoA thiolase (thiolase), 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGCS), and HMG-CoA reductase. The thiolase reaction is highly endergonic. In the thiolase/HMGCS complex, the endergonic thiolase reaction is directly coupled to the exergonic 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase reaction. A third protein spatially connects both enzymes. The two enzymes share the same substrate-binding site. Genomic information indicates that the presence of a thiolase/HMGCS complex is common in most of archaea and many bacteria
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physiological function
Vitis vinifera x Vitis vinifera
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involved in terpenoid metabolism
physiological function
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involved in terpenoid metabolism
physiological function
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enzyme overexpression up-regulates 3-hydroxy-3-methylglutaryl-CoA reductase, sterol methyltransferase 2, delta-24 sterol reductase, C-22 sterol desaturase, and brassinosteroid-6-oxidase 2, leading to enhanced sterol content and stress tolerance in Arabidopsis. Enzyme overexpressing Arabidopsis seeds germinate approximately 1 day earlier than wild type seeds. Enzyme overexpressing Arabidopsis seedlings show enhanced resistance to Botrytis cinerea, and detached leaves are delayed in H2O2-induced cell death
physiological function
the enzyme is involved in the mevalonate pathway in archaea. Archaea are characterized by cell membrane lipids that contain, as a major component, polyisoprenoids in ether linkages to glycerol rather than the ester-linked fatty acids that characterize membranes of other organisms. Archaeal polyisoprenoids derive from isopentenyl 5-diphosphate produced by enzymes of the mevalonate pathway
physiological function
enzyme-overexpressing tobacco plants produce more seeds that germinate earlier and show increased growth compared to the control
physiological function
oligodendrocyte progenitor cell migration and myelin gene expression require enzyme function of 3-hydroxy-3-methylglutaryl CoA synthase I
physiological function
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the enzyme is involved in the mevalonate pathway in archaea. Archaea are characterized by cell membrane lipids that contain, as a major component, polyisoprenoids in ether linkages to glycerol rather than the ester-linked fatty acids that characterize membranes of other organisms. Archaeal polyisoprenoids derive from isopentenyl 5-diphosphate produced by enzymes of the mevalonate pathway
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