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malfunction
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enzyme deficiency is a rare metabolic disease of autosomal recessive inheritance characterized by intermittent ketoacidotic episodes with onset in the infant period and decline with age, overview
malfunction
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mutants with deletion of isoform Acat1 exhibit defect in virulence only, while mutants of isoform Acat2 are characterized by reduction in growth and virulence
malfunction
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mutants with deletion of isoform Acat1 exhibit defect in virulence only, while mutants of isoform Acat2 are characterized by reduction in growth and virulence
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metabolism
the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-ketoacyl-CoA to acyl-CoA
metabolism
the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-ketoacyl-CoA to acyl-CoA
metabolism
the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-oxoacyl-CoA to acyl-CoA
metabolism
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the enzyme of the biosynthetic pathway for polyhydroxyalkanoates
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
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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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metabolism
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the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-ketoacyl-CoA to acyl-CoA
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metabolism
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the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-oxoacyl-CoA to acyl-CoA
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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
isoform AACT2 function is required for embryogenesis and for normal male gamete transmission. RNAi lines that express reduced levels of isoform AACT2 show pleiotropic phenotypes, including reduced apical dominance, elongated life span and flowering duration, sterility, dwarfing, reduced seed yield and shorter root length. The reduced stature is caused by a reduction in cell size and fewer cells, and male sterility is caused by loss of the pollen coat and premature degeneration of the tapetal cells. The roots of AACT2 RNAi plants show quantitative and qualitative alterations in phytosterol profiles. These phenotypes and biochemical alterations are reversed when AACT2 RNAi plants are grown in the presence of mevalonate
physiological function
over-expressing transgenic plants show salinity tolerance comparable with empty vector transformed plants and enhanced production of squalene without alteration in the 3-hydroxy-3-methylglutaryl-CoA reductase activity in salt-stress conditions
physiological function
plants lacking isoform AACT1 function are completely viable and show no apparent growth phenotypes
physiological function
the enzyme is involved in autotrophic carbon fixation
physiological function
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
physiological function
the enzyme is responsible for supplying the precursors for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
physiological function
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the activity of isoform Acat1 promotes virulence in the rice blast fungus
physiological function
the enzyme is involved in fatty acid metabolism, for energy or physical requirements to adapt to the host
physiological function
Erg10A is essential for the survival of Neosartoya fumigata. The reduced expression of Erg10A leads to severe morphological defects and increased susceptibility to oxidative and cell wall stresses
physiological function
expression in Saccharomyces cerevisiae complements a yeast Erg10knockout mutant
physiological function
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the activity of isoform Acat1 promotes virulence in the rice blast fungus
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physiological function
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Erg10A is essential for the survival of Neosartoya fumigata. The reduced expression of Erg10A leads to severe morphological defects and increased susceptibility to oxidative and cell wall stresses
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physiological function
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the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
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physiological function
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the enzyme is responsible for supplying the precursors for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
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physiological function
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the enzyme is involved in autotrophic carbon fixation
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additional information
similar to other degradative thiolases, enzyme ReH16_B0759 functions as a dimer, and the monomer comprises three subdomains. Unlike enzyme ReH16_A1887, a substantial structural change is not observed upon the binding of the CoA substrate in enzyme ReH16_B0759. At the active site of the enzyme highly conserved residues Cys89, His347, and Cys377are located near the thiol-group of CoA
additional information
the enzyme functions as a dimer, and the monomer comprises three subdomains I, II, and III. The structural comparison between the apoform and the CoA-bound form reveals that the enzyme undergoes a structural change in the lid-subdomain III upon the binding of the CoA substrate. The CoA molecule is stabilized by hydrogen bonding with positively charged residues Lys18, Arg210, and Arg217, and residues Thr213 and Gln151 aid its binding as well. At the enzyme's active site highly conserved residues, Cys91, His348, and Cys378, are located near the thiol-group of CoA, indicating that enzyme ReH16_A1887 might catalyze the thiolase reaction in a way similar to other thiolases. In the vicinity of the covalent nucleophile Cys91, a hydrophobic hole that might serve as a binding site for the acyl-group of 3-oxoacyl-CoA. Subdomains I and II harbor the active site residues: Cys91 in subdomain I, and His348 and Cys378 in subdomain II
additional information
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similar to other degradative thiolases, enzyme ReH16_B0759 functions as a dimer, and the monomer comprises three subdomains. Unlike enzyme ReH16_A1887, a substantial structural change is not observed upon the binding of the CoA substrate in enzyme ReH16_B0759. At the active site of the enzyme highly conserved residues Cys89, His347, and Cys377are located near the thiol-group of CoA
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additional information
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the enzyme functions as a dimer, and the monomer comprises three subdomains I, II, and III. The structural comparison between the apoform and the CoA-bound form reveals that the enzyme undergoes a structural change in the lid-subdomain III upon the binding of the CoA substrate. The CoA molecule is stabilized by hydrogen bonding with positively charged residues Lys18, Arg210, and Arg217, and residues Thr213 and Gln151 aid its binding as well. At the enzyme's active site highly conserved residues, Cys91, His348, and Cys378, are located near the thiol-group of CoA, indicating that enzyme ReH16_A1887 might catalyze the thiolase reaction in a way similar to other thiolases. In the vicinity of the covalent nucleophile Cys91, a hydrophobic hole that might serve as a binding site for the acyl-group of 3-oxoacyl-CoA. Subdomains I and II harbor the active site residues: Cys91 in subdomain I, and His348 and Cys378 in subdomain II
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