N-acetylneuraminate synthase | |||||||||
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![]() N-acetylneuraminic acid synthase dimer, Neisseria meningitidis | |||||||||
Identifiers | |||||||||
EC no. | 2.5.1.56 | ||||||||
CAS no. | 37290-66-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a N-acetylneuraminate synthase (EC 2.5.1.56) is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are phosphoenolpyruvate, N-acetyl-D-mannosamine, and H2O, whereas its two products are phosphate and N-acetylneuraminate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:N-acetyl-D-mannosamine C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming). Other names in common use include (NANA)condensing enzyme, N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating), and NeuAc synthase. This enzyme participates in aminosugars metabolism.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1WVO.
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 biochemical reactions to release the energy stored in nutrients through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins. The chemical energy released is available under the form of ATP. 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.
Oxaloacetic acid (also known as oxalacetic acid or OAA) is a crystalline organic compound with the chemical formula HO2CC(O)CH2CO2H. Oxaloacetic acid, in the form of its conjugate base oxaloacetate, is a metabolic intermediate in many processes that occur in animals. It takes part in gluconeogenesis, the urea cycle, the glyoxylate cycle, amino acid synthesis, fatty acid synthesis and the citric acid cycle.
Glucose-1,6-bisphosphate synthase is a type of enzyme called a phosphotransferase and is involved in mammalian starch and sucrose metabolism. It catalyzes the transfer of a phosphate group from 1,3-bisphosphoglycerate to glucose-1-phosphate, yielding 3-phosphoglycerate and glucose-1,6-bisphosphate.
The enzyme indole-3-glycerol-phosphate synthase (IGPS) (EC 4.1.1.48) catalyzes the chemical reaction
The enzyme N-acetylneuraminate lyase catalyzes the chemical reaction
In enzymology, a 2-ethylmalate synthase (EC 2.3.3.6) is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-isopropylmalate synthase (EC 2.3.3.13) is an enzyme that catalyzes the chemical reaction
In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction
In enzymology, a 1-deoxy-d-xylulose-5-phosphate synthase (EC 2.2.1.7) is an enzyme in the non-mevalonate pathway that catalyzes the chemical reaction
In enzymology, a 3-deoxy-8-phosphooctulonate synthase (EC 2.5.1.55) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acylneuraminate-9-phosphate synthase (EC 2.5.1.57) is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylglucosamine 1-carboxyvinyltransferase is an enzyme that catalyzes the first committed step in peptidoglycan biosynthesis of bacteria:
In enzymology, a N-acylmannosamine kinase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme that catalyzes the chemical reaction
Pyruvate, phosphate dikinase, or PPDK is an enzyme in the family of transferases that catalyzes the chemical reaction
In enzymology, a pyruvate, water dikinase (EC 2.7.9.2) is an enzyme that catalyzes the chemical reaction
3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. Since it is the first enzyme in the shikimate pathway, it controls the amount of carbon entering the pathway. Enzyme inhibition is the primary method of regulating the amount of carbon entering the pathway. Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme.
5-enolpyruvylshikimate-3-phosphate (EPSP) synthase is an enzyme produced by plants and microorganisms. EPSPS catalyzes the chemical reaction:
N,N'-diacetyllegionaminate synthase (EC 2.5.1.101, neuB (gene), legI (gene)) is an enzyme with systematic name phosphoenolpyruvate:2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose 1-(2-carboxy-2-oxoethyl)transferase. This enzyme catalyses the following chemical reaction
4-Hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7, dihydrodipicolinate synthase, dihydropicolinate synthetase, dihydrodipicolinic acid synthase, L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing), dapA (gene)) is an enzyme with the systematic name L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming). This enzyme catalyses the following chemical reaction