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Citrate synthase (E.C. 2.3.3.1 (previously 4.1.3.7)) is an enzyme that exists in nearly all living cells. It functions as a pace-making enzyme in the first step of the citric acid cycle (or Krebs cycle). [5] Citrate synthase is located within eukaryotic cells in the mitochondrial matrix, but is encoded by nuclear DNA rather than
In molecular biology, the citrate synthase family of proteins includes the enzymes citrate synthase EC 2.3.3.1, and the related enzymes 2-methylcitrate synthase EC 2.3.3.5 and ATP citrate lyase EC 2.3.3.8. Citrate synthase is a member of a small family of enzymes that can directly form a carbon-carbon bond without the presence of metal ion ...
N 2-citryl-N 6-acetyl-N 6-hydroxylysine synthase (EC 6.3.2.38, N(alpha)-citryl-N(epsilon)-acetyl-N(epsilon)-hydroxylysine synthase, iucA (gene)) is an enzyme with systematic name citrate:N 6-acetyl-N 6-hydroxy-L-lysine ligase (ADP-forming).
Oxoglutarate dehydrogenase is a key control point in the citric acid cycle. It is inhibited by its products, succinyl CoA and NADH.A high energy charge in the cell will also be inhibitive.
ATP citrate synthase (also ATP citrate lyase (ACLY)) is an enzyme that in animals catalyzes an important step in fatty acid biosynthesis. [2] By converting citrate to acetyl-CoA , the enzyme links carbohydrate metabolism , which yields citrate as an intermediate , with fatty acid biosynthesis , which consumes acetyl-CoA. [ 3 ]
However, in the presence of high levels of malate and NAD +, citrate can stimulate the production of oxaloacetate. Although malate dehydrogenase is typically considered a reversible enzyme, it is believed that there is an allosteric regulatory site on the enzyme where citrate can bind to and drive the reaction equilibrium in either direction. [19]
In enzymology, a citrate (Re)-synthase (EC 2.3.3.3) is an enzyme that catalyzes the chemical reaction acetyl-CoA + H 2 O + oxaloacetate ⇌ {\displaystyle \rightleftharpoons } citrate + CoA The 3 substrates of this enzyme are acetyl-CoA , H 2 O , and oxaloacetate , whereas its two products are citrate and CoA .
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1CM5, 1H16, 1H17, 1H18, 1MZO, 1QHM, 2PFL, and 3PFL. Pyruvate formate lyase is a homodimer made of 85 kDa, 759-residue subunits. It has a 10-stranded beta/alpha barrel motif into which is inserted a beta finger that contains major catalytic residues.