succinylglutamate desuccinylase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.1.96 | ||||||||
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 succinylglutamate desuccinylase (EC 3.5.1.96) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are N-succinyl-L-glutamate and H2O, whereas its two products are succinate and L-glutamate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-succinyl-L-glutamate amidohydrolase. Other names in common use include N2-succinylglutamate desuccinylase, SGDS, and AstE. This enzyme participates in arginine and proline metabolism.
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.
In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.
N-Acetylglutamate synthase (NAGS) is an enzyme that catalyses the production of N-acetylglutamate (NAG) from glutamate and acetyl-CoA.
In enzymology, a succinate-semialdehyde dehydrogenase (SSADH) (EC 1.2.1.24) is an enzyme that catalyzes the chemical reaction
In enzymology, a succinylglutamate-semialdehyde dehydrogenase (EC 1.2.1.71) is an enzyme that catalyzes the chemical reaction
In enzymology, a succinyl-CoA:(R)-benzylsuccinate CoA-transferase is an enzyme that catalyzes the chemical reaction
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In enzymology, a N-formylglutamate deformylase (EC 3.5.1.68) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-succinylarginine dihydrolase (EC 3.5.3.23) is an enzyme that catalyzes the chemical reaction
In enzymology, a succinyl-diaminopimelate desuccinylase (EC 3.5.1.18) is an enzyme that catalyzes the chemical reaction
In enzymology, an arginine N-succinyltransferase (EC 2.3.1.109) is an enzyme that catalyzes the chemical reaction
In enzymology, an acetylornithine transaminase (EC 2.6.1.11) is an enzyme that catalyzes the chemical reaction
In enzymology, a diaminobutyrate-2-oxoglutarate transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, a succinylornithine transaminase (EC 2.6.1.81) is an enzyme that catalyzes the chemical reaction
The gabT RNA motif is the name of a conserved RNA structure identified by bioinformatics whose function is unknown. The gabT motif has been detected exclusively in bacteria within the genus Pseudomonas, and is found only upstream of gabT genes, and downstream to gabD genes.
In molecular biology, members of the ArgJ protein family are bifunctional protein that catalyses the first and fifth steps in arginine biosynthesis. The structure has been determined for glutamate N-acetyltransferase 2, an ArgJ-like protein from Streptomyces clavuligerus.
In molecular biology, the arginine repressor (ArgR) is a repressor of prokaryotic arginine deiminase pathways.