604-98-8

Basic information

• Product Name: S-(hydrogen succinyl)coenzyme A
• Synonyms: Succinyl-coenzyme A; Coenzyme A, S-(hydrogen butanedioate); S-(Hydrogen succinyl)coenzyme A; 1-[5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-10,14,19-trioxo-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphadocosan-22-oic acid 3,5-dioxide (non-preferred name); (9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-10,14,19-trioxo-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphadocosan-22-oic acid 3,5-dioxide (non-preferred name)
• CAS NO: 604-98-8
• Molecular Formula: C₂₅H₄₀N₇O₁₉P₃S
• Molecular Weight: 867.6069
• EINECS: 210-079-5
• Mol File: 604-98-8.mol
• Article Data: 6

Chemical Properties

• Density: 1.91g/cm³
• Refractive Index: 1.719
• CAS DataBase Reference: S-(hydrogen succinyl)coenzyme A(CAS DataBase Reference)
• NIST Chemistry Reference: S-(hydrogen succinyl)coenzyme A(604-98-8)
• EPA Substance Registry System: S-(hydrogen succinyl)coenzyme A(604-98-8)

Safety Data

• Hazardous Substances Data: 604-98-8(Hazardous Substances Data)

Usage

General Description

S-(hydrogen succinyl)coenzyme A is a chemical compound that plays a critical role in the citric acid cycle, also known as the Krebs cycle, which is a central pathway for energy production in the cells of living organisms. This coenzyme A derivative is involved in the conversion of succinyl-CoA to succinate, a key step in the cycle that produces high-energy molecules such as ATP and NADH. S-(hydrogen succinyl)coenzyme A is also important in the synthesis of heme, a crucial component of hemoglobin and other hemoproteins involved in oxygen transport and storage. Additionally, this compound participates in the regulation of cellular metabolism and has implications for various metabolic disorders. Thus, S-(hydrogen succinyl)coenzyme A is vital for energy production and various cellular processes essential for life.

Upstream product

• 108-30-5 succinic acid anhydride 
• 18439-24-2 coenzyme A lithium salt 
• 110-15-6 succinic acid 
• 72-89-9 acetylcoenzyme A 
• 1264-45-5 (2RS)-methylmalonyl-CoA 
• 85-61-0 coenzyme A 

Downstream Products

• 72-89-9 acetylcoenzyme A 
• 317-66-8 S-propionyl-coenzyme-A 
• 3131-84-8 glutaryl-CoA 
• 524-14-1 S-(hydrogen malonyl)coenzyme A 
• 92256-33-2 N-(2-indol-3-yl-ethyl)-succinamic acid 
• 106-60-5 ALA 
• 85-61-0 coenzyme A 

Relevant articles and documents

Tyrosine 89 accelerates Co-carbon bond homolysis in methylmalonyl-CoA mutase

The contribution of the active-site residue, Y89, to the trillion-fold acceleration of Co-carbon bond homolysis rate in the methylmalonyl-CoA mutase-catalyzed reaction has been evaluated by site-directed mutagenesis. Conversion of Y89 to phenylalanine or alanine results in a 103-fold diminution of kcat and suppression of the overall kinetic isotope effect. The spectrum of the enzyme under steady-state conditions reveals the presence of AdoCbl but no cob(II)alamin. Together, these results are consistent with homolysis becoming completely rate determining in the forward direction in the two mutants and points to the role of Y89 as a molecular wedge in accelerating Co-carbon bond cleavage.

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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.