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ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
ATP + citrate + CoA
acetyl-CoA + oxaloacetate + ADP + phosphate
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
citrate + CoA + ATP
acetyl-CoA + oxaloacetate + ADP + phosphate
-
Substrates: -
Products: -
?
dATP + citrate + CoA
dADP + phosphate + acetyl-CoA + oxaloacetate
GTP + citrate + CoA
GDP + phosphate + acetyl-CoA + oxaloacetate
N6-etheno-adenosine triphosphate + citrate + CoA
N6-etheno-adenosine diphosphate + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
oxaloacetate + acetyl-CoA + ADP + phosphate
citrate + ATP + CoA
Substrates: -
Products: -
?
additional information
?
-
ADP + phosphate + acetyl-CoA + oxaloacetate

ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ATP + citrate + CoA

acetyl-CoA + oxaloacetate + ADP + phosphate
-
Substrates: -
Products: -
ir
ATP + citrate + CoA
acetyl-CoA + oxaloacetate + ADP + phosphate
-
Substrates: -
Products: -
ir
ATP + citrate + CoA

ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: enzyme generates cytosolic acetyl-CoA
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the enzyme is regulated by the carbon source present in the medium
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the cytosolic enzyme may provide acetyl-coenzyme A for the mevalonate pathway or fatty acid elongation
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the plastidic enzyme is proposed to function for the supply of acetyl-coenzyme A for lipid biosynthesis de novo
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: key enzyme of CO2 fixation by reductive tricarboxylic acid
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the first step of the reaction is reversible
Products: -
ir
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: enzyme regulates both the direction and carbon flux of the carbon dioxide-fixing reductive tricarboxylic acid cycle
Products: -
ir
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: enzyme is induced by starvation-refeeding regimen
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: one of the key enzymes of lipogenesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: cleaves citrate with inversion of configuration
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: specific for citrate
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: one of the key enzymes of lipogenesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
ir
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
r
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: acetyl-CoA is produced in mitochondria, but it cannot cross the mitochondrial membranes to the cytosol. Instead, citrate is exported from mitochondria. In the cytosol, ATP-citrate lyase (ACLY; EC 2.3.3.8) catalyses the reaction to produce acetyl-CoA and oxaloacetate from citrate and ATP
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: the enzyme synthesizes cytosolic acetyl coenzyme A (acetyl-CoA), a fundamental cellular building block
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: ATP citrate lyase is an important enzyme linking carbohydrate to lipid metabolism by generating acetyl-CoA from citrate for fatty acid and cholesterol biosynthesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: the enzyme catalyzes the formation of cytosolic acetyl CoA, the starting material for de novo lipid and cholesterol biosynthesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: the enzyme is a major source of nucleocytosolic acetyl-CoA, a fundamental building block of carbon metabolism in eukaryotes
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: the enzyme links carbohydrate and lipid metabolism
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: acetyl-coenzyme A (acetyl-CoA) generated by ATP citrate lyase (ACL) is utilized to acetylate histone H3 at MyoD regulatory regions, resulting in increased MyoD expression and improved muscle regeneration after injury
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: the enzyme links glycolysis to lipid metabolism
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
r
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the synthase activity is less than 0.5% of the ATP:citrate lyase activity
Products: -
r
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the synthase activity is less than 0.5% of the ATP:citrate lyase activity
Products: -
r
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the cytosolic enzyme may provide acetyl-coenzyme A for the mevalonate pathway or fatty acid elongation
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: specific for ATP
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: specific for ATP
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: essential enzyme for generating acetyl-CoA, a key metabolite for the first step in fatty acid synthesis and for histone acetylation. Regulation of the enzyme activity is a potentially important point of control for cell cycle regulation in the myeloid lineage
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the cytosolic enzyme may provide acetyl-coenzyme A for the mevalonate pathway or fatty acid elongation
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
488184, 488185, 488186, 488188, 488190, 488191, 488192, 488193, 488195, 488196, 488197, 488199, 488200, 488201, 488205, 488206, 488207, 488208, 488210, 488212, 488213, 488214, 488215, 488220, 488221, 488223 Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: specific for citrate
Products: -
r, ?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the enzyme is engaged in the transport of acetyl groups from mitochondria to cytosol. On the metabolic pathway from carbohydrate to lipid it is the first enzyme which is exclusively biosynthetic
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: one of the key enzymes of lipogenesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the enzyme catalyzes the first cytoplasmic step in the synthesis of long-chain fatty acids in mammalian tissues
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the enzyme is responsible for production of cytoplasmic acetyl-CoA for lipogenesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: key enzyme for lipid accumulation
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: specific for ATP
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: specific for ATP
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: specific for ATP
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: specific for CoA
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: possibly plays a role in providing acetyl-CoA for lipid biosynthesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the cytosolic enzyme may provide acetyl-coenzyme A for the mevalonate pathway or fatty acid elongation
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the plastidic enzyme is proposed to function for the supply of acetyl-coenzyme A for lipid biosynthesis de novo
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
dATP + citrate + CoA

dADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: 40% of the activity with ATP
Products: -
?
dATP + citrate + CoA
dADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
dATP + citrate + CoA
dADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
GTP + citrate + CoA

GDP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
GTP + citrate + CoA
GDP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
additional information

?
-
-
Substrates: enzyme is a nonredundant source of cytosolic acetyl-CoA
Products: -
?
additional information
?
-
-
Substrates: only the complex of Acl1 and Acl2 shows AT P-citrate lyase activity, no enzyme activities are detected with the individual protein
Products: -
?
additional information
?
-
-
Substrates: only the complex of Acl1 and Acl2 shows AT P-citrate lyase activity, no enzyme activities are detected with the individual protein
Products: -
?
additional information
?
-
Substrates: dATP may substitute for ATP, no substrate: malate, isocitrate, succinate, acetate
Products: -
?
additional information
?
-
-
Substrates: dATP may substitute for ATP, no substrate: malate, isocitrate, succinate, acetate
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
ATP + citrate + CoA
acetyl-CoA + oxaloacetate + ADP + phosphate
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
oxaloacetate + acetyl-CoA + ADP + phosphate
citrate + ATP + CoA
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is a nonredundant source of cytosolic acetyl-CoA
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate

ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA + oxaloacetate
ATP + citrate + CoA
-
Substrates: -
Products: -
?
ATP + citrate + CoA

acetyl-CoA + oxaloacetate + ADP + phosphate
-
Substrates: -
Products: -
ir
ATP + citrate + CoA
acetyl-CoA + oxaloacetate + ADP + phosphate
-
Substrates: -
Products: -
ir
ATP + citrate + CoA

ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: enzyme generates cytosolic acetyl-CoA
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the enzyme is regulated by the carbon source present in the medium
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the cytosolic enzyme may provide acetyl-coenzyme A for the mevalonate pathway or fatty acid elongation
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the plastidic enzyme is proposed to function for the supply of acetyl-coenzyme A for lipid biosynthesis de novo
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: key enzyme of CO2 fixation by reductive tricarboxylic acid
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: enzyme regulates both the direction and carbon flux of the carbon dioxide-fixing reductive tricarboxylic acid cycle
Products: -
ir
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: enzyme is induced by starvation-refeeding regimen
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: one of the key enzymes of lipogenesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: one of the key enzymes of lipogenesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: acetyl-CoA is produced in mitochondria, but it cannot cross the mitochondrial membranes to the cytosol. Instead, citrate is exported from mitochondria. In the cytosol, ATP-citrate lyase (ACLY; EC 2.3.3.8) catalyses the reaction to produce acetyl-CoA and oxaloacetate from citrate and ATP
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: the enzyme synthesizes cytosolic acetyl coenzyme A (acetyl-CoA), a fundamental cellular building block
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: ATP citrate lyase is an important enzyme linking carbohydrate to lipid metabolism by generating acetyl-CoA from citrate for fatty acid and cholesterol biosynthesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: the enzyme catalyzes the formation of cytosolic acetyl CoA, the starting material for de novo lipid and cholesterol biosynthesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: the enzyme is a major source of nucleocytosolic acetyl-CoA, a fundamental building block of carbon metabolism in eukaryotes
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: the enzyme links carbohydrate and lipid metabolism
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: acetyl-coenzyme A (acetyl-CoA) generated by ATP citrate lyase (ACL) is utilized to acetylate histone H3 at MyoD regulatory regions, resulting in increased MyoD expression and improved muscle regeneration after injury
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: the enzyme links glycolysis to lipid metabolism
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
r
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the cytosolic enzyme may provide acetyl-coenzyme A for the mevalonate pathway or fatty acid elongation
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: essential enzyme for generating acetyl-CoA, a key metabolite for the first step in fatty acid synthesis and for histone acetylation. Regulation of the enzyme activity is a potentially important point of control for cell cycle regulation in the myeloid lineage
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the cytosolic enzyme may provide acetyl-coenzyme A for the mevalonate pathway or fatty acid elongation
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the enzyme is engaged in the transport of acetyl groups from mitochondria to cytosol. On the metabolic pathway from carbohydrate to lipid it is the first enzyme which is exclusively biosynthetic
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: one of the key enzymes of lipogenesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the enzyme catalyzes the first cytoplasmic step in the synthesis of long-chain fatty acids in mammalian tissues
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the enzyme is responsible for production of cytoplasmic acetyl-CoA for lipogenesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: key enzyme for lipid accumulation
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: possibly plays a role in providing acetyl-CoA for lipid biosynthesis
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: -
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the cytosolic enzyme may provide acetyl-coenzyme A for the mevalonate pathway or fatty acid elongation
Products: -
?
ATP + citrate + CoA
ADP + phosphate + acetyl-CoA + oxaloacetate
-
Substrates: the plastidic enzyme is proposed to function for the supply of acetyl-coenzyme A for lipid biosynthesis de novo
Products: -
?
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(1S,2S)-1,2-dihydroxypropane-1,2,3-tricarboxylic acid
-
50% inhibition at 0.00015 mM
(2E)-3-phenylprop-2-en-1-yl 2-[[(3,5-dichloro-2-hydroxyphenyl)sulfonyl]amino]benzoate
-
50% inhibition at 0.00034 mM
(2R)-2-[(2S)-8-(3,5-dichlorophenyl)-2-hydroxyoctyl]-2-hydroxysuccinic acid
-
50% inhibition at 0.0021 mM
1,3,8-trihydroxy-2-(3-methoxyphenyl)-6-methylanthracene-9,10-dione
-
-
1,3,8-trihydroxy-2-(4-methoxyphenyl)-6-methylanthracene-9,10-dione
-
-
1,3,8-trihydroxy-2-iodo-6-methylanthracene-9,10-dione
-
-
1,3,8-trihydroxy-6-methyl-2-(1-methyl-1H-pyrazol-4-yl)anthracene-9,10-dione
-
-
1,3,8-trihydroxy-6-methyl-2-(3-methylphenyl)anthracene-9,10-dione
-
-
1,3,8-trihydroxy-6-methyl-2-(pyridin-3-yl)anthracene-9,10-dione
-
-
1,3,8-trihydroxy-6-methyl-2-phenylanthracene-9,10-dione
-
-
1,3,8-trihydroxy-6-methyl-2-[(morpholin-4-yl)methyl]anthracene-9,10-dione
-
-
1,3,8-trihydroxy-6-methyl-2-[(piperidin-1-yl)methyl]anthracene-9,10-dione
-
-
1,3,8-trihydroxy-6-methyl-2-[[methyl(phenyl)amino]methyl]anthracene-9,10-dione
-
-
1,3-dibromo-2,4,5-trihydroxy-7-methylanthracene-9,10-dione
-
-
1-chloro-2,4,5-trihydroxy-7-methylanthracene-9,10-dione
-
-
2,4,5-trihydroxy-7-methyl-1,3-di(pyridin-3-yl)anthracene-9,10-dione
-
-
2-chloro-1,3,8-trihydroxy-6-methylanthracen-9(10H)-one
-
-
2-chloro-1,3,8-trihydroxy-6-methylanthracene-9,10-dione
-
-
2-hydroxy-2-[(S-methylsulfonimidoyl)methyl]butanedioic acid
-
weak, reversible
3,3,14,14-tetramethylhexadecanedioic acid
-
i.e. Medica-16
3,5-dichloro-2-hydroxy-N-(4-methoxybiphenyl-3-yl)benzenesulfonamide
3,5-dichloro-N-(2,4,6-triphenyl-phenyl)-2-hydroxybenzenesulfonamide
-
50% inhibition at 0.00019 mM
3,5-dichloro-N-(3,5-di-tert-butylphenyl)-2-hydroxybenzenesulfonamide
-
50% inhibition at 0.0011 mM
3-(1,3-benzoxazol-5-yl)-5,7-dihydroxy-9-methyl-3,4-dihydro-2H-anthra[2,3-e][1,3]oxazine-6,11-dione
-
-
4-chloro-1,3,8-trihydroxy-6-methylanthracen-9(10H)-one
-
-
4-[[(2-hexyl-6-oxo-7,8,9,10-tetrahydro-6H-dibenzo[b,d]pyran-3-yl)oxy]methyl]-5-methylfuran-2-carboxylic acid
0.01 mM, 95% inhibition. 0.1 mM, 100% inhibition
-
4-[[(3,4-dibenzyl-2-oxo-2H-1-benzopyran-7-yl)oxy]methyl]-5-methylfuran-2-carboxylic acid
0.01 mM, 3% inhibition. 0.1 mM, 64% inhibition
-
4-[[(3,4-dibenzyl-6-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]methyl]-5-methylfuran-2-carboxylic acid
0.01 mM, 32% inhibition. 0.1 mM, 84% inhibition
-
4-[[(6-hexyl-2-oxo-4-phenyl-2H-1-benzopyran-7-yl)oxy]methyl]-5-methylfuran-2-carboxylic acid
0.01 mM, 53% inhibition. 0.1 mM, 92% inhibition
-
5,7-dihydroxy-9-methyl-3-phenyl-3,4-dihydro-2H-anthra[2,3-e][1,3]oxazine-6,11-dione
-
5-methyl-2-(1-methylethyl)cyclohexyl 2-[[(3,5-dichloro-2-hydroxyphenyl)sulfonyl]amino]benzoate
-
50% inhibition at 0.00037 mM
5-methyl-4-[[(2-oxo-4-phenyl-2H-1-benzopyran-7-yl)oxy]methyl]furan-2-carboxylic acid
0.01 mM,32% inhibition. 0.1 mM, 84% inhibition
-
5-methyl-4-[[(2-oxo-4-phenyl-6-propyl-2H-1-benzopyran-7-yl)oxy]methyl]furan-2-carboxylic acid
0.01 mM, 97% inhibition. 0.1 mM, 97% inhibition
-
5-methyl-4-[[(4-methyl-2-oxo-3-phenyl-2H-1-benzopyran-7-yl)oxy]methyl]furan-2-carboxylic acid
0.01 mM, 45% inhibition. 0.1 mM, 101% inhibition
-
5-methyl-4-[[(4-methyl-6-oxo-7,8,9,10-tetrahydro-6H-dibenzo[b,d]pyran-3-yl)oxy]methyl]furan-2-carboxylic acid
0.01 mM, 17% inhibition. 0.1 mM, 90% inhibition
-
5-[(2,3-dimethylbenzene-1-sulfonyl)amino]-2-methyl-1-benzofuran-3-carboxylic acid
0.01 mM, 11% inhibition. 0.1 mM, 43% inhibition
-
5-[(4-fluoro-2-methylbenzene-1-sulfonyl)amino]-2-methyl-1-benzofuran-3-carboxylic acid
0.01 mM, 3% inhibition. 0.1 mM, 9% inhibition
-
5-[(4-fluorobenzene-1-sulfonyl)amino]-2-phenyl-1-benzofuran-3-carboxylic acid
0.01 mM, 19% inhibition. 0.1 mM, 70% inhibition
-
5-[(4-methyl-3-nitrobenzene-1-sulfonyl)amino]-2-phenyl-1-benzofuran-3-carboxylic acid
0.01 mM,21% inhibition. 0.1 mM, 89% inhibition
-
5-[(4-methylbenzene-1-sulfonyl)amino]-2-phenyl-1-benzofuran-3-carboxylic acid
0.01 mM, 23% inhibition. 0.1 mM, 93% inhibition
-
5-[(benzenesulfonyl)amino]-2-phenyl-1-benzofuran-3-carboxylic acid
0.01 mM, 11% inhibition. 0.1 mM, 56% inhibition
-
5-[[(3,4-dibenzyl-2-oxo-2H-1-benzopyran-7-yl)oxy]methyl]furan-2-carboxylic acid
0.01 mM, 9% inhibition. 0.1 mM, 49% inhibition
-
5-[[(4-methyl-6-oxo-7,8,9,10-tetrahydro-6H-dibenzo[b,d]pyran-3-yl)oxy]methyl]furan-2-carboxylic acid
0.01 mM, 18% inhibition. 0.1 mM, 88% inhibition
-
6,7-dibenzyl-2-methyl-5-[(4-methylbenzene-1-sulfonyl)amino]-1-benzofuran-3-carboxylic acid
0.01 mM, 12% inhibition. 0.1 mM, 42% inhibition
-
6,7-dibenzyl-5-[(4-ethylbenzene-1-sulfonyl)amino]-2-methyl-1-benzofuran-3-carboxylic acid
0.01 mM, 42% inhibition. 0.1 mM, 97% inhibition
-
6,7-dibenzyl-5-[(4-fluorobenzene-1-sulfonyl)amino]-2-methyl-1-benzofuran-3-carboxylic acid
0.01 mM, 28% inhibition. 0.1 mM, 95% inhibition
-
6,7-dibenzyl-5-[(4-tert-butylbenzene-1-sulfonyl)amino]-2-methyl-1-benzofuran-3-carboxylic acid
0.01 mM, 16% inhibition. 0.1 mM, 59% inhibition
-
D-fructose 2,6-diphosphate
-
18% inhibition
D-glucose 6-phosphate
-
-
diethyldicarbonate
-
the addition of 0.5 mM ATP in the preincubation reaction mixture provided complete protection of enzyme activity from inactivation by diethyldicarbonate
GSSG
-
inactivation involves formation of a protein-protein disulfide rather than a protein-glutathione complex
herbacetin
strong noncompetitive inhibitor
isochlorogenic acid C
noncompetitive inhibitor. The compound directly binds to the enzyme and improves its stability in the heating process
L-Leu
-
2 mM, 20% inhibition
luteolin
strong inhibitor
luteolin 7-O-glucuronide
-
malonyl-CoA
-
0.4 mM, 70% inhibition
methyl 3-chloro-5-(N-(4,6-difluoro-[1,1'-biphenyl]-3-yl)sulfamoyl)-4-hydroxybenzoate
myricetin
strong inhibitor
Nexletol
bempedoic acid or ETC-1002
-
quercetin
strong inhibitor
radicicol biotinylated at the C-17 position
-
no inhibition with the derivative biotinylated at the C-18 position
scutellarein
strong inhibitor
stewartiacid G
(3S,4S,5R,8R,9R,10S,11S,14S,17R,18R,19S,20R)-11alpha-methoxy-3beta,12-dihydroxy-urs-12-en-23-oic acid, moderate inhibition
-
stewartiacid K
(3S*,4S*,5R*,8R*,9R*,10S*,11S*,14S*,17R*,18R*,19S*,20R*,7'R*,8'R*)-11alpha,12-[2-(hydroxymethyl)-3-(4-hydroxy-3-methoxyphenyl)ethane-1,2-dioxy]-3beta-acetoxy-urs-12-en-23-oic acid, moderate inhibition. The absolute configurations of stewartiacid K is still open, however, it can be assigned based on biogenetic considerations (*)
-
stewartiacid L
(3S,4S,5R,8R,9R,10S,11S,14S,17R,18R,19S,20R,7'S,8'R)-11alpha,12-[3-(hydroxymethyl)-2-(4-hydroxy-3-methoxyphenyl)ethane-1,2-dioxy]-3beta-acetoxy-urs-12-en-23-oic acid, moderate inhibition
-
additional information
not inhibited by ferulic acid, isoferulic acid, caffeic acid diglucoside, chlorogenic acid, neochlorogenic acid, protocatechuic acid, and cryptochlorogenic acid
-
(+)-2,2-difluorocitrate

-
-
(+)-2,2-difluorocitrate
-
-
(-)-2,2-difluorocitrate

-
-
(-)-2,2-difluorocitrate
-
-
(-)-Hydroxycitrate

-
potent inhibitor
(-)-Hydroxycitrate
-
potent inhibitor
3,5-dichloro-2-hydroxy-N-(4-methoxybiphenyl-3-yl)benzenesulfonamide

-
50% inhibition of enzyme at 0.00013 mM, 50% inhibition of total lipid synthesis in HepG-2 cells at 0.008 mM, no cytotoxicity up to 0.05 mM
3,5-dichloro-2-hydroxy-N-(4-methoxybiphenyl-3-yl)benzenesulfonamide
-
shows an oral availability of 55%, but a half-life of only 2.1 h. After 20 days of treatment, there is a modest lowering of both plasma cholesterol and triglycerides in high-fat fed mice
ADP

-
2 mM, 82% inhibition
ADP
-
competitive inhibitor of ATP
bempedoic acid

-
bempedoic acid
i.e. ETC-1002 is a first-in-class, prodrug-based direct competitive inhibitor of ATP citrate lyase which regulates lipid metabolism by upregulating hepatic LDL receptor (LDLr) expression and activity. Pharmacological inhibition of ACLY by bempedoic acid, prevents dyslipidemia and attenuates atherosclerosis in hypercholesterolemic ApoE-/- mice, LDLr-/- mice, and LDLr-/- miniature pigs
BMS-303141

-
-
BMS-303141
specific inhibitor
BMS-303141
strong inhibitor
BMS-303141
specific inhibitor
dATP

-
weak
Glu

-
10 mM, inhibition is unlikely to be due to any direct interaction of L-Glu and ATP citrate lyase
Hydroxycitrate

-
Hydroxycitrate
-
competitive
lauroyl-CoA

-
10 mM, 52% inhibition
methyl 3-chloro-5-(N-(4,6-difluoro-[1,1'-biphenyl]-3-yl)sulfamoyl)-4-hydroxybenzoate

i.e. NDI-091143, the structure of the full-length human ACLY homo-tetramer in complex NDI-091143 is determined by cryo-electron microscopy. The compound is located in an allosteric, mostly hydrophobic cavity next to the citrate-binding site, and requires extensive conformational changes in the enzyme that indirectly disrupt citrate binding
methyl 3-chloro-5-(N-(4,6-difluoro-[1,1'-biphenyl]-3-yl)sulfamoyl)-4-hydroxybenzoate
i.e. NDI-091143, allosteric inhibition
myristoyl-CoA

-
10 mM, 5% inhibition
oleoyl-CoA

-
10 mM, 21% inhibition
oxaloacetate

-
-
palmitoyl-CoA

-
10 mM, 5% inhibition
radicicol

-
noncompetitive inhibitor
radicicol
-
noncompetitive inhibitor
radicicol
-
noncompetitive
SB-201076

-
-
SB-204990

-
-
SB-204990
in addition to lowering lipids by inhibiting ACLY, the chemical inhibitor SB-204990 also displays tumor suppressive effects
stearoyl-CoA

-
10 mM, 45% inhibition
Tartrate

-
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0.0212
1,3,8-trihydroxy-2-(3-methoxyphenyl)-6-methylanthracene-9,10-dione
Homo sapiens
pH 8.0, 30°C
-
0.0188
1,3,8-trihydroxy-2-(4-methoxyphenyl)-6-methylanthracene-9,10-dione
Homo sapiens
pH 8.0, 30°C
-
0.0075
1,3,8-trihydroxy-2-iodo-6-methylanthracene-9,10-dione
Homo sapiens
pH 8.0, 30°C
-
0.0133
1,3,8-trihydroxy-6-methyl-2-(1-methyl-1H-pyrazol-4-yl)anthracene-9,10-dione
Homo sapiens
pH 8.0, 30°C
-
0.03
1,3,8-trihydroxy-6-methyl-2-(3-methylphenyl)anthracene-9,10-dione
Homo sapiens
pH 8.0, 30°C
-
0.0211
1,3,8-trihydroxy-6-methyl-2-(pyridin-3-yl)anthracene-9,10-dione
Homo sapiens
pH 8.0, 30°C
-
0.0029
1,3-dibromo-2,4,5-trihydroxy-7-methylanthracene-9,10-dione
Homo sapiens
pH 8.0, 30°C
-
0.0096
1-chloro-2,4,5-trihydroxy-7-methylanthracene-9,10-dione
Homo sapiens
pH 8.0, 30°C
-
0.0235
2,4,5-trihydroxy-7-methyl-1,3-di(pyridin-3-yl)anthracene-9,10-dione
Homo sapiens
pH 8.0, 30°C
-
0.000283
2-chloro-1,3,8-trihydroxy-6-methylanthracen-9(10H)-one
Homo sapiens
pH 8.0, 30°C
-
0.0126
2-chloro-1,3,8-trihydroxy-6-methylanthracene-9,10-dione
Homo sapiens
pH 8.0, 30°C
-
0.0038
4-chloro-1,3,8-trihydroxy-6-methylanthracen-9(10H)-one
Homo sapiens
pH 8.0, 30°C
-
0.0041
5-methyl-4-[[(2-oxo-4-phenyl-6-propyl-2H-1-benzopyran-7-yl)oxy]methyl]furan-2-carboxylic acid
Homo sapiens
pH 8.0, temperature not specified in the publication
-
0.0119
5-methyl-4-[[(4-methyl-2-oxo-3-phenyl-2H-1-benzopyran-7-yl)oxy]methyl]furan-2-carboxylic acid
Homo sapiens
pH 8.0, temperature not specified in the publication
-
0.0138
6,7-dibenzyl-5-[(4-ethylbenzene-1-sulfonyl)amino]-2-methyl-1-benzofuran-3-carboxylic acid
Homo sapiens
pH 8.0, temperature not specified in the publication
-
0.01911
apigenin
Homo sapiens
at pH 8.0 and 37°C
0.0128
austroyunone A
Homo sapiens
pH and temperature not specified in the publication
-
0.00006 - 0.00094
BMS-303141
0.00026
BSM-303141
Homo sapiens
at pH 8.0 and 37°C
-
0.03376
caffeic acid
Homo sapiens
at 37°C, pH not specified in the publication
0.02364
catechin
Homo sapiens
at pH 8.0 and 37°C
0.00129
cyanidin
Homo sapiens
at pH 8.0 and 37°C
0.00302
dodovisin A
Homo sapiens
at pH 8.0 and 37°C
-
0.0026
dodovisin F
Homo sapiens
at pH 8.0 and 37°C
-
0.03163
epicatechin
Homo sapiens
at pH 8.0 and 37°C
0.00031
gossypetin
Homo sapiens
at pH 8.0 and 37°C
0.0005
herbacetin
Homo sapiens
at pH 8.0 and 37°C
0.00153
hyperoside
Homo sapiens
at pH 8.0 and 37°C
0.00056
isochlorogenic acid B
Homo sapiens
at 37°C, pH not specified in the publication
0.00014
isochlorogenic acid C
Homo sapiens
at 37°C, pH not specified in the publication
0.00186
isoorientin
Homo sapiens
at pH 8.0 and 37°C
0.00214
isoquercetin
Homo sapiens
at pH 8.0 and 37°C
0.04974
isorhamnetin
Homo sapiens
at pH 8.0 and 37°C
0.01016
kaempferol
Homo sapiens
at pH 8.0 and 37°C
0.00143
lonicerin
Homo sapiens
at pH 8.0 and 37°C
-
0.00064
luteolin
Homo sapiens
at pH 8.0 and 37°C
0.00147
luteolin 7-O-glucuronide
Homo sapiens
at pH 8.0 and 37°C
0.0098
methyl gallate
Homo sapiens
at 37°C, pH not specified in the publication
0.00407
morin
Homo sapiens
at pH 8.0 and 37°C
0.00057
myricetin
Homo sapiens
at pH 8.0 and 37°C
0.00238
oblatone A
Homo sapiens
pH and temperature not specified in the publication
-
0.0021
oblatone C
Homo sapiens
pH and temperature not specified in the publication
-
0.0112
oblatone E
Homo sapiens
pH and temperature not specified in the publication
-
0.0081
oblatone F
Homo sapiens
pH and temperature not specified in the publication
-
0.0128
oblatone H
Homo sapiens
pH and temperature not specified in the publication
-
0.0051
parrotiagallol E
Homo sapiens
at 37°C, pH not specified in the publication
-
0.00086
quercetin
Homo sapiens
at pH 8.0 and 37°C
0.00071
scutellarein
Homo sapiens
at pH 8.0 and 37°C
0.00377
scutellarin
Homo sapiens
at pH 8.0 and 37°C
0.0125
stewartiacid G
Homo sapiens
at 37°C, pH not specified in the publication
-
0.0028
stewartiacid K
Homo sapiens
at 37°C, pH not specified in the publication
-
0.0106
stewartiacid L
Homo sapiens
at 37°C, pH not specified in the publication
-
0.00024
strictic acid
Homo sapiens
at pH 8.0 and 37°C
-
0.00254
taxifolin
Homo sapiens
at pH 8.0 and 37°C
0.00057
vincetoxicoside B
Homo sapiens
at pH 8.0 and 37°C
-
0.00006
BMS-303141

Homo sapiens
pH and temperature not specified in the publication
0.000377
BMS-303141
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0004
BMS-303141
Homo sapiens
at 37°C, pH not specified in the publication
0.000442
BMS-303141
Homo sapiens
pH 8.0, 30°C
0.00094
BMS-303141
Homo sapiens
-
-
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-
-
-
brenda
subunits; synonym Aspergillus nidulans
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
-
-
brenda
-
-
-
brenda
-
-
-
brenda
culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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cultivar Ponkan
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cultivar Satsuma mandarin
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cultivar Xiangshui
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large subunit of enzyme; expression on Escherichia coli
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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anamorph Fusarium graminearum
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anamorph Fusarium graminearum
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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CBS 1809
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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CBS 13
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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ecotype Columbia
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subunit ACLB1; ecotype Columbia-0 and Landsberg erecta
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subunits; synonym Aspergillus nidulans
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recombinant enzyme
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culture dependent and independent analyses of 16S rRNA and ATP citrate lyase genes: a comparison of microbial communities from different black smoker chimneys on the Mid-Atlantic Ridge. Comparative analyses of the ATP citrate lyase encoding genes from natural microbial communities suggest that Epsilonproteobacteria are the dominant primary producers using the reverse TCA cycle at Rainbow, while Aquificales of the genera Desulfurobacterium and Persephonella are prevalent in the Broken Spur chimney
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forma thiosulfatophilum, strain IC and strain L
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gene acLB, beta-subunit; subunit ORF1, product of gene acLB, both subunits ORF1 and ORF2 are essential for enzyme activity
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755722, 756189, 756333, 756335, 756395, 756645, 756693, 757200, 757232, 757453, 757794, 757803, 757804, 758267, 758518, 758520, 776857, 776942, 777174, 777332, 777415, 777420, 777591, 777744, 777834, 778699, 778904, 778905, 778911, 779254, 779350 UniProt
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male renal stone patients, supplementary diet with potassium-magnesium citrate
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patients suffering diabetes
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recombinant enzyme
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CBS 1809
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33352, 488184, 488185, 488186, 488188, 488190, 488191, 488192, 488193, 488195, 488196, 488197, 488199, 488200, 488201, 488205, 488206, 488207, 488208, 488210, 488212, 488213, 488214, 488215, 488220, 488221, 488223, 685373 -
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CBS 13
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evolution

structural studies unmask a fundamental evolutionary relationship that links citrate synthase, the first enzyme of the oxidative Krebs cycle, to an ancestral tetrameric citryl-CoA lyase module that operates in the reverse Krebs cycle. This molecular transition marked a key step in the evolution of metabolism on Earth
evolution
structural studies unmask a fundamental evolutionary relationship that links citrate synthase, the first enzyme of the oxidative Krebs cycle, to an ancestral tetrameric citryl-CoA lyase module that operates in the reverse Krebs cycle. This molecular transition marked a key step in the evolution of metabolism on Earth
malfunction

loss of ATP-citrate lyase results in severe developmental effects, with the production of asexual spores (conidia) being greatly reduced and a complete absence of sexual development
malfunction
inhibition of the enzyme suppresses in vitro glioblastoma cell migration, clonogenicity and brain invasion under glycolytic conditions and enhances the suppressive effects of a Met inhibitor on cell migration
malfunction
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overexpression of the enzyme is observed in nonalcoholic fatty liver disease. Increased enzyme activity is associated with hypocituria, nonalcoholic fatty liver disease, and tumor cell growth. Decreased enzyme activity is associated with type 2 diabetes. ACLY knockdown or inhibition leads to a decrease in glucose-induced insulin secretion
malfunction
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deletion of the enzyme results in a complete loss of self and female fertility as well as a reduction in asexual reproduction, virulence, and trichothecene production. Although lipid synthesis is not affected by enzyme deletion, histone acetylation is dramatically reduced in the enzyme deletion mutants during sexual development
malfunction
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ATP citrate lyase knockdown induces proliferation arrest, cell-cycle arrest, and apoptosis in cancer cells and results in elevated expression of acyl-CoA synthetase short-chain family member 2
malfunction
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enzyme knockdown triggers cellular senescence and activation of tumor suppressor p53
malfunction
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enzyme activity inhibition as well as gene silencing lead to reduced nitric oxide, reactive oxygen species and prostaglandin E2 inflammatory mediators
malfunction
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enzyme inactivation decreases fatty acid synthesis by 60 to 80%
malfunction
ATP citrate lyase silencing impairs myoblast and satellite cell differentiation, and it is accompanied by a decrease in fast myosin heavy chain isoforms and MYOD
malfunction
upon genetic deletion of Acly, the gene coding for ATP-citrate lyase, cells remain viable and proliferate, although at an impaired rate. In the absence of ACLY, cells upregulate ACSS2 and utilize exogenous acetate to provide acetyl-CoA for de novo lipogenesis and histone acetylation. A physiological level of acetate is sufficient for cell viability and abundant acetyl-CoA production, although histone acetylation levels remain low in ACLY-deficient cells unless supplemented with high levels of acetate. ACLY-deficient adipocytes accumulate lipid in vivo, exhibit increased acetyl-CoA and malonyl-CoA production from acetate, and display some differences in fatty acid content and synthesis. Engagement of acetate metabolism is a crucial, although partial, mechanism of compensation for ACLY deficiency
malfunction
siRNA knockdown of ATP citrate lyase limits cancer cell proliferation and reduces cancer stemness
malfunction
decrease in ATP level, energy charge, and fatty acid content in mutant edt1 anthers
malfunction
ATP citrate lyase silencing impairs myoblast and satellite cell differentiation, and it is accompanied by a decrease in fast myosin heavy chain isoforms and MYOD
malfunction
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although loss of Drosophila ATP citrate lyase (DmATPCL) reduces levels of acetyl-CoA, it does not affect global histone acetylation and gene expression, suggesting that its role in histone acetylation is either partially redundant in Drosophila or compensated by alternative pathways. Depletion of DmATPCL affects spindle organization, cytokinesis, and fusome assembly during male meiosis
malfunction
enzyme deficiency leads to impaired growth and histone acetylation
malfunction
deletion of the enzyme gene in mice results in embryonic lethality
malfunction
enzyme-deficient macrophages show hyperinflammatory gene signatures in response to acute lipopolysaccharide stimulation in vitro. Also during obesity, both chronic low-grade inflammation and whole-body metabolic homeostasis remain largely unaltered in mice with enzyme-deficient myeloid cells. Macrophage-specific enzyme deletion does not affect the severity of experimental autoimmune encephalomyelitis. Macrophage enzyme deficiency does not worsen acute and chronic inflammatory responses in vivo
malfunction
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enzyme depletion affects the organization of acrosome and affects the Golgi apparatuses in primary spermatocy
malfunction
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upon a knockout of the enzyme gene, lipid content in Rhodotorula toruloides IFO0880 decreases from 50 to 9% of its dry cell weight in glucose medium and causes severe growth defects (reduced specific growth rate, changes in cell morphology)
malfunction
enzyme downregulation inhibits gastric cancer cell growth in vitro and in vivo. Downregulation of the enzyme reduces lipid accumulation and inhibits gastric cancer cell proliferation, migration, and invasion in vitro
malfunction
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genetic enzyme ablation prevents PTEN loss-induced T-cell acute lymphoblastic leukemia/lymphoma development and abrogates apoptosis resistance in mutant double-positive progenitors
malfunction
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enzyme silencing in cotton leads to cell death at newly-grown leaves and stem apexes. Simultaneously, in subunit ACLB-silenced plants, transcription factors related to senescence including SGR, WRKY23 and Osl57 are activated. Knockdown of ACLB genes leads to hypersensitive response-like cell death in cotton seedlings. The resistance to Verticillium dahliae infection in the Arabidopsis mutant aclb-2 is enhanced without causing strong cell death. Ectopic expression of subunit ACLB-2 in Arabidopsis weakens its resistance to Verticillium dahliae
malfunction
enzyme inhibition rewires endothelial cell gluco-lipogenic metabolism in response to lipopolysaccharide
malfunction
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loss of ATP-citrate lyase results in severe developmental effects, with the production of asexual spores (conidia) being greatly reduced and a complete absence of sexual development
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malfunction
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deletion of the enzyme results in a complete loss of self and female fertility as well as a reduction in asexual reproduction, virulence, and trichothecene production. Although lipid synthesis is not affected by enzyme deletion, histone acetylation is dramatically reduced in the enzyme deletion mutants during sexual development
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malfunction
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upon a knockout of the enzyme gene, lipid content in Rhodotorula toruloides IFO0880 decreases from 50 to 9% of its dry cell weight in glucose medium and causes severe growth defects (reduced specific growth rate, changes in cell morphology)
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metabolism

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involved in lung cancer pathogenesis
metabolism
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the enzyme is involved in citrate metabolism
metabolism
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the enzyme is involved in citrate metabolism
metabolism
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DNA methyltransferase 1 is regulated by ATP-citrate lyase
metabolism
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the enzyme plays an essential role in fatty acid synthesis
metabolism
essential enzyme for generating acetyl-CoA, a key metabolite for the first step in fatty acid synthesis and for histone acetylation. Regulation of the enzyme activity is a potentially important point of control for cell cycle regulation in the myeloid lineage
metabolism
the enzyme synthesizes cytosolic acetyl coenzyme A (acetyl-CoA), a fundamental cellular building block
metabolism
ATP citrate lyase is an important enzyme linking carbohydrate to lipid metabolism by generating acetyl-CoA from citrate for fatty acid and cholesterol biosynthesis
metabolism
the enzyme plays a critical role in epigenetic regulation of diabetic renal fibrosis. It is essential for high glucose-induced histone hyperacetylation and fibrogenic gene upregulation in mesangial cells
metabolism
the enzyme catalyzes the formation of cytosolic acetyl CoA, the starting material for de novo lipid and cholesterol biosynthesis
metabolism
the enzyme links energy metabolism provided by catabolic pathways to biosynthesis. ACLY plays a pivotal role in cancer metabolism through the potential deprivation of cytosolic citrate, a process promoting glycolysis through the enhancement of the activities of PFK 1 and 2 with concomitant activation of oncogenic drivers such as PI3K/AKT which activate ACLY and the Warburg effect in a feed-back loop
metabolism
enzyme in the de novo lipogenesis pathway. The enzyme is required for low molecular weight cyclin E-mediated transformation, migration, and invasion of breast cancer cells in vitro along with tumor growth in vivo
metabolism
the enzyme controls a glucose-to-acetate metabolic switch
metabolism
the enzyme plays a critical role in generating cytosolic acetyl CoA, a key building block for de novo fatty acid and cholesterol biosynthesis
metabolism
the enzyme is an epigenetic regulator that promotes renal ectopic lipid accumulation and fibrogenesis leading to renal injury in obesity. Induction of ATP-citrate lyase in in the kidney of overweight or obese patients with chronic kidney disease is associated with increased ectopic lipid accumulation, glomerulosclerosis, and albuminuria. Acetyl-CoA is the substrate for de novo lipogenesis as well as for histone acetylation. By raising acetyl-CoA concentration ATP-citrate lyase promotes H3K9/14 and H3K27 hyperacetylation leading to up-regulation of several rate-limiting lipogenic enzymes and fibrogenic factors. On the other hand, the excess acetyl-CoA generated as a result of ATP-citrate lyase induction provides the substrate for these lipogenic enzymes to drive de novo lipogenesis leading to ectopic lipid accumulation, a detrimental event toward renal injury
metabolism
regulatory role of ACLY activity in chondrocyte matrix homeostasis by modulation of the nucleocytosolic pool of acetyl-CoA, which impacted on catabolic and anabolic responses via post-translational and epigenetic modifications. Increased ACLY activity in osteoarthritis chondrocytes increases nucleocytosolic acetyl-CoA, leading to increased matrix catabolism via dysregulated histone and transcription factor acetylation
metabolism
the enzyme is a major source of nucleocytosolic acetyl-CoA, a fundamental building block of carbon metabolism in eukaryotes
metabolism
modulation of ACLY expression correlates with the development and progressions of various chronic diseases such as neurodegenerative diseases, cardiovascular diseases, diabetes, obesity, inflammation, and cancer. Inhibition of ACLY activity modulates the glycolysis and lipogenesis processes and stimulates normal physiological functions
metabolism
ATP-citrate lyase is a central metabolic enzyme. The acetyl-CoA product is crucial for the metabolism of fatty acids, the biosynthesis of cholesterol, and the acetylation and prenylation of proteins
metabolism
the enzyme links carbohydrate and lipid metabolism
metabolism
acetyl-coenzyme A (acetyl-CoA) generated by ATP citrate lyase (ACL) is utilized to acetylate histone H3 at MyoD regulatory regions, resulting in increased MyoD expression and improved muscle regeneration after injury
metabolism
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the enzyme is required for a proper male meiosis
physiological function

ATP-citrate lyase is required for development in Aspergillus nidulans
physiological function
ATP citrate lyase is a positive regulator of glycolytic function in glioblastomas
physiological function
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the enzyme is essentially required for embryonic development. Increased enzyme activity is found in the fetal development of the brain
physiological function
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ATP citrate lyase is required for normal sexual and asexual development in Gibberella zeae
physiological function
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the enzyme regulates mitochondrial function and cardiolipin synthesis and content in skeletal muscle
physiological function
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the enzyme regulates cellular senescence via an AMPK- and p53-dependent pathway
physiological function
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isoforms Acl1 and Acl2 coordinately modulate the cytoplasmic acetyl-CoA levels to regulate growth, development, and citric acid synthesis in Aspergillus niger
physiological function
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enzyme overexpression in Arabidopsis is associated with a 30% increase in wax on stems, while overexpression of a chimeric homomeric enzyme in the laticifer of roots of dandelion leads to a 4 and 2fold increase in rubber and triterpene content, respectively
physiological function
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the enzyme is essential for macrophage inflammatory response
physiological function
ATP citrate lyase plays a key role in regulating mitochondrial function, as well as glucose and lipid metabolism in skeletal muscle. The enzyme increases myoblast and satellite cell differentiation in vitro. It increases MYOD expression by acetyl-H3(K9/14/27) enrichment at the MYOD promoter. It acts downstream of IGF-1 to stimulate myogenesis. IT improves muscle regeneration following cardiotoxin-induced injury
physiological function
the enzyme (EDT1) is involved in the tapetum programmed cell death process
physiological function
ATP citrate lyase plays a key role in regulating mitochondrial function, as well as glucose and lipid metabolism in skeletal muscle. The enzyme increases myoblast and satellite cell differentiation in vitro. It increases MYOD expression by acetyl-H3(K9/14/27) enrichment at the MYOD promoter. It acts downstream of IGF-1 to stimulate myogenesis. IT improves muscle regeneration following cardiotoxin-induced injury
physiological function
the enzyme promotes endothelial cell gluco-lipogenic metabolism and proinflammatory response through acetylation-mediated c-Myc transcription. The enzyme participates in promoting inflammatory response and multiple organ injury in sepsis
physiological function
the enzyme exerts inhibitory effects on proinflammatory cytokine expression in response to lipopolysaccharide without affecting cholesterol-handling genes. The enzyme retains functionality in the absence of Akt/protein kinase A-mediated phosphorylation in human myeloid cells. Loss of enzyme activity may elicit long-term adaptive mechanisms, increasing inflammatory responses
physiological function
the enzyme impacts certain adaptive immune responses through metabolic and epigenetic remodeling. Enzyme-dependent lipid biosynthesis supports immature myeloid cell proliferation. The enzyme is an essential mediator of macrophage inflammatory responses. The enzyme is essential for growth and proliferation of cancer cells by supporting membrane biosynthesis through de novo fatty acid synthesis. In addition to its classical function in the provision of acetyl-CoA for de novo lipogenesis, the enzyme contributes to epigenetic regulation in B lymphocytes through histone acetylation
physiological function
myeloid enzyme regulates macrophage inflammatory responses in vitro without altering inflammatory disease outcomes
physiological function
the enzyme is important for myelin maintenance rather than myelin formation. In addition, the enzyme is required to maintain expression of a myelin-associated gene program and to inhibit activation of the latent Schwann cell injury program
physiological function
the enzyme plays potential roles in immunometabolic regulation in sepsis
physiological function
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the enzyme plays a role in the assembly of Golgi-derived structures during Drosophila spermatogenesis. The enzyme is required for spindle organization, cytokinesis, and fusome assembly during male meiosis, mainly due to is activity on fatty acid biosynthesis
physiological function
the enzyme is essential for plant development. Acetyl-CoA synthesized by the enzyme is used for sporopollenin biosynthesis in the tapetum
physiological function
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the enzyme is crucial for the fatty acid synthesis and growth in Rhodotorula toruloides IFO0880
physiological function
the enzyme mediates glycolytic inhibition of vesicular suppressor of cytokine signaling 3 secretion
physiological function
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enzyme overexpression enhances lipid accumulation and docosahexaenoic acid production in Schizochytrium sp.
physiological function
the enzyme is required for the transformation of thymic immature progenitors upon phosphatase and tensin homolog (PTEN) loss. Enzyme activation represents a metabolic vulnerability with therapeutic potential in high-risk PTEN-altered human T-cell acute lymphoblastic leukemia
physiological function
the enzyme promotes endothelial cell gluco-lipogenic metabolism and proinflammatory response through acetylation-mediated c-Myc transcription. The enzyme participates in promoting inflammatory response and multiple organ injury in sepsis
physiological function
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ATP-citrate lyase is required for development in Aspergillus nidulans
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physiological function
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ATP citrate lyase is required for normal sexual and asexual development in Gibberella zeae
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physiological function
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isoforms Acl1 and Acl2 coordinately modulate the cytoplasmic acetyl-CoA levels to regulate growth, development, and citric acid synthesis in Aspergillus niger
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physiological function
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the enzyme is crucial for the fatty acid synthesis and growth in Rhodotorula toruloides IFO0880
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48 h after exhaustion of nitrogen in the culture, the enzyme shows marked decrease (84%) in activity. The enzyme activity decreases in a time period of 20-100 h during lipid accumulation
CitERF6 trans-activates the promoter of enzyme subunit CitAclalpha1. In the presence of CitERF6, CitAclalpha1 promoter activity is significantly enhanced, with approximately 2.6fold induction
enzyme activity increases with dissolved oxygen and upon ammonium depletion in an ammonium-limited culture
enzyme mRNA and protein levels markedly (about 2.5fold) and quickly increase in activated macrophages. Tumour necrosis factor alpha and interferon gamma upregulate enzyme gene expression
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high glucose upregulates ATP-citrate lyase expression
higher levels of enzyme are detected in sera of pediatric patients with sepsis than that of healthy children
highly induced in ob/ob BTBR mice
highly induced in the kidney of overweight or obese patients with chronic kidney disease. Induction is associated with increased ectopic lipid accumulation, glomerulosclerosis, and albuminuria. Acetyl-CoA is the substrate for de novo lipogenesis as well as for histone acetylation. By raising acetyl-CoA concentration ATP-citrate lyase promotes H3K9/14 and H3K27 hyperacetylation leading to up-regulation of several rate-limiting lipogenic enzymes and fibrogenic factors. On the other hand, the excess acetyl-CoA generated as a result of ATP-citrate lyase induction provides the substrate for these lipogenic enzymes to drive de novo lipogenesis leading to ectopic lipid accumulation, a detrimental event toward renal injury
in mesangial cells, the enzyme is synergistically induced by high glucose, palmitate, and TNF-alpha via NF-kapaB and PKA pathways
levels of phosphorylated enzyme are increased in the lung, kidney, and liver from septic mice, which are inhibited by BMS-303141 administration
low molecular weight cyclin E upregulates enzymatic activity, subsequently increasing lipid droplet formation, thereby providing cells with essential building blocks to support growth
mRNA transcript levels decrease during normal macrophage differentiation from bone marrow precursors
overexpressed in many cancers. ACLY transcription is promoted by SREBP1
phosphatase and tensin homolog (PTEN)-altered T-cell acute lymphoblastic leukemia cells activate the enzyme. PTEN deletion activates the enzyme in preleukemic thymic cells
sterol regulatory element binding protein-1 up-regulates the enzyme at mRNA level via Akt signaling
the enzyme activity increases in the first 20 h during lipid accumulation
the enzyme expression decreases during lemon fruit development
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the enzyme expression is induced upon high carbohydrate exposure
the enzyme expression is repressed during high fat feeding
the enzyme expression is upregulated in gastric cancer tissue
the enzyme is overexpressed in cancer cells
there are about 3fold increased levels of the enzyme in glioblastoma pseudopodia compared to unmigrated cells
transcription of genes aclA and aclB is repressed by growth on acetate or ethanol
48 h after exhaustion of nitrogen in the culture, the enzyme shows marked decrease (84%) in activity. The enzyme activity decreases in a time period of 20-100 h during lipid accumulation

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48 h after exhaustion of nitrogen in the culture, the enzyme shows marked decrease (84%) in activity. The enzyme activity decreases in a time period of 20-100 h during lipid accumulation
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CitERF6 trans-activates the promoter of enzyme subunit CitAclalpha1. In the presence of CitERF6, CitAclalpha1 promoter activity is significantly enhanced, with approximately 2.6fold induction

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CitERF6 trans-activates the promoter of enzyme subunit CitAclalpha1. In the presence of CitERF6, CitAclalpha1 promoter activity is significantly enhanced, with approximately 2.6fold induction
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enzyme activity increases with dissolved oxygen and upon ammonium depletion in an ammonium-limited culture

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enzyme activity increases with dissolved oxygen and upon ammonium depletion in an ammonium-limited culture
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levels of phosphorylated enzyme are increased in the lung, kidney, and liver from septic mice, which are inhibited by BMS-303141 administration

levels of phosphorylated enzyme are increased in the lung, kidney, and liver from septic mice, which are inhibited by BMS-303141 administration
phosphatase and tensin homolog (PTEN)-altered T-cell acute lymphoblastic leukemia cells activate the enzyme. PTEN deletion activates the enzyme in preleukemic thymic cells

phosphatase and tensin homolog (PTEN)-altered T-cell acute lymphoblastic leukemia cells activate the enzyme. PTEN deletion activates the enzyme in preleukemic thymic cells
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sterol regulatory element binding protein-1 up-regulates the enzyme at mRNA level via Akt signaling

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sterol regulatory element binding protein-1 up-regulates the enzyme at mRNA level via Akt signaling
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the enzyme activity increases in the first 20 h during lipid accumulation

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the enzyme activity increases in the first 20 h during lipid accumulation
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transcription of genes aclA and aclB is repressed by growth on acetate or ethanol

transcription of genes aclA and aclB is repressed by growth on acetate or ethanol
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