3131-84-8

Usage

Uses

Used in Pharmaceutical Industry:
Glutaryl-coenzyme A is used as an intermediate in the metabolism of certain amino acids, such as lysine, tryptophan, and hydroxylysine. It is involved in the breakdown of these amino acids through the corresponding catabolic pathways, which are essential for the proper functioning of the human body.
Used in Biochemical Research:
Glutaryl-coenzyme A is used as a research tool in the field of biochemistry to study the mechanisms of various metabolic pathways and enzyme functions. It helps researchers understand the role of coenzyme A and its interactions with different substrates.
Used in Enzyme Assays:
Glutaryl-coenzyme A is used as a substrate in enzyme assays to measure the activity of specific enzymes involved in the metabolism of glutaric acid. This helps in the diagnosis of certain genetic disorders and the evaluation of enzyme deficiencies.
Used in Drug Development:
Glutaryl-coenzyme A may be used in the development of new drugs targeting metabolic pathways related to glutaric acid metabolism. By modulating the activity of enzymes involved in these pathways, it could potentially lead to the development of therapeutic agents for various diseases.

Upstream product

• 110-94-1 1,5-pentanedioic acid 
• 72-89-9 acetylcoenzyme A 
• 604-98-8 succinyl-coenzyme A 
• 85-61-0 coenzyme A 

Relevant academic research and scientific papers

Identification of an α-Oxoamine Synthase and a One-Pot Two-Step Enzymatic Synthesis of α-Amino Ketones

Alb29, an α-oxoamine synthase involved in albogrisin biosynthesis in Streptomyces albogriseolus MGR072, was characterized and responsible for the incorporation of l-glutamate to acyl-coenzyme A substrates. Combined with Alb29 and Mgr36 (an acyl-coenzyme A ligase), a one-pot enzymatic system was established to synthesize seven α-amino ketones. When these α-amino ketones were fed into the alb29 knockout strain Δalb29, respectively, the albogrisin analogs with different side chains were observed.

Crystal structures of Acetobacter aceti succinyl-coenzyme A (CoA):Acetate CoA-transferase reveal specificity determinants and illustrate the mechanism used by class i CoA-transferases

Coenzyme A (CoA)-transferases catalyze transthioesterification reactions involving acyl-CoA substrates, using an active-site carboxylate to form covalent acyl anhydride and CoA thioester adducts. Mechanistic studies of class I CoA-transferases suggested that acyl-CoA binding energy is used to accelerate rate-limiting acyl transfers by compressing the substrate thioester tightly against the catalytic glutamate [White, H., and Jencks, W. P. (1976) J. Biol. Chem. 251, 1688-1699]. The class I CoA-transferase succinyl-CoA:acetate CoA-transferase is an acetic acid resistance factor (AarC) with a role in a variant citric acid cycle in Acetobacter aceti. In an effort to identify residues involved in substrate recognition, X-ray crystal structures of a C-terminally His6-tagged form (AarCH6) were determined for several wild-type and mutant complexes, including freeze-trapped acetylglutamyl anhydride and glutamyl-CoA thioester adducts. The latter shows the acetate product bound to an auxiliary site that is required for efficient carboxylate substrate recognition. A mutant in which the catalytic glutamate was changed to an alanine crystallized in a closed complex containing dethiaacetyl-CoA, which adopts an unusual curled conformation. A model of the acetyl-CoA Michaelis complex demonstrates the compression anticipated four decades ago by Jencks and reveals that the nucleophilic glutamate is held at a near-ideal angle for attack as the thioester oxygen is forced into an oxyanion hole composed of Gly388 NH and CoA N2″. CoA is nearly immobile along its entire length during all stages of the enzyme reaction. Spatial and sequence conservation of key residues indicates that this mechanism is general among class I CoA-transferases.