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The citric acid cycle —also known as the Krebs cycle, Szent-Györgyi-Krebs cycle or the TCA cycle (tricarboxylic acid cycle)—is a series of chemical reactions to release stored energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins. The Krebs cycle is used by organisms that respire (as opposed to organisms that ferment) to generate energy, either by anaerobic respiration or aerobic respiration. In addition, the cycle provides precursors of certain amino acids, as well as the reducing agent NADH, that are used in numerous other reactions. Its central importance to many biochemical pathways suggests that it was one of the earliest components of metabolism. Even though it is branded as a 'cycle', it is not necessary for metabolites to follow only one specific route; at least three alternative segments of the citric acid cycle have been recognized.
A transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups from one molecule to another. They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes.
In biochemistry and metabolism, beta oxidation (also β-oxidation) is the catabolic process by which fatty acid molecules are broken down in the cytosol in prokaryotes and in the mitochondria in eukaryotes to generate acetyl-CoA, which enters the citric acid cycle, and NADH and FADH2, which are co-enzymes used in the electron transport chain. It is named as such because the beta carbon of the fatty acid undergoes oxidation to a carbonyl group. Beta-oxidation is primarily facilitated by the mitochondrial trifunctional protein, an enzyme complex associated with the inner mitochondrial membrane, although very long chain fatty acids are oxidized in peroxisomes.
Aspartoacylase is a hydrolytic enzyme that in humans is encoded by the ASPA gene. ASPA catalyzes the deacylation of N-acetyl-l-aspartate (N-acetylaspartate) into aspartate and acetate. It is a zinc-dependent hydrolase that promotes the deprotonation of water to use as a nucleophile in a mechanism analogous to many other zinc-dependent hydrolases. It is most commonly found in the brain, where it controls the levels of N-acetyl-l-aspartate. Mutations that result in loss of aspartoacylase activity are associated with Canavan disease, a rare autosomal recessive neurodegenerative disease.
In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acetylglucosaminylphosphatidylinositol deacetylase (EC 3.5.1.89) is an enzyme that catalyzes the chemical reaction
In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides.
In enzymology, a 2-isopropylmalate synthase (EC 2.3.3.13) is an enzyme that catalyzes the chemical reaction
In enzymology, a histidine N-acetyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a malate synthase (EC 2.3.3.9) is an enzyme that catalyzes the chemical reaction
In enzymology, a glycoprotein 3-alpha-L-fucosyltransferase (EC 2.4.1.214) is an enzyme that catalyzes the chemical reaction
Dipeptidase 1 (DPEP1), or renal dipeptidase, is a membrane-bound glycoprotein responsible for hydrolyzing dipeptides. It is found in the microsomal fraction of the porcine kidney cortex. It exists as a disulfide-linked homodimer that is glygosylphosphatidylinositol (GPI)-anchored to the renal brush border of the kidney. The active site on each homodimer is made up of a barrel subunit with binuclear zinc ions that are bridged by the Gly125 side-chain located at the bottom of the barrel.
Carnosinemia is a rare autosomal recessive metabolic disorder caused by a deficiency of carnosinase, a dipeptidase.
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:3-(alpha-D-mannosyl)-beta-D-mannosyl-glycoprotein 2-beta-N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction
Galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,5/1,6-galactofuranosyltransferase is an enzyme with systematic name UDP-alpha-D-galactofuranose:beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol 4-beta/5-beta-D-galactofuranosyltransferase. This enzyme catalyses the following chemical reaction
Endo-α-N-acetylgalactosaminidase (EC 3.2.1.97, endo-α-acetylgalactosaminidase, endo-α-N-acetyl-D-galactosaminidase, mucinaminylserine mucinaminidase, D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase, endo-α-GalNAc-ase, D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase) is an enzyme with systematic name glycopeptide-D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase. This enzyme catalyses the following chemical reaction
Mannosylglycoprotein endo-beta-mannosidase is an enzyme. This enzyme catalyses the following chemical reaction:
Xaa-His dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Xaa-Pro dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Beta-Ala-His dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction
References
- ↑ Jones NR (May 1955). "The free amino acids of fish; 1-methylhistidine and beta-alanine liberation by skeletal muscle anserinase of codling (Gadus callarias)". The Biochemical Journal. 60 (1): 81–7. PMC 1215656 . PMID 14363188.
- ↑ Baslow MH, Lenney JF (February 1967). "Alpha-N-acetyl-L-histidine amidohydrolase activity from the brain of the skipjack tuna Katsuwonus pelamis". Canadian Journal of Biochemistry. 45 (2): 337–40. doi:10.1139/o67-037. PMID 6067033.
- ↑ Lenney JF, Baslow MH, Sugiyama GH (1978). "Similarity of tuna N-acetylhistidine deacetylase and cod fish anserinase". Comparative Biochemistry and Physiology. B, Comparative Biochemistry. 61 (2): 253–8. doi:10.1016/0305-0491(78)90171-2. PMID 318374.
