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 
• 85-61-0 coenzyme A 
• 1264-45-5 (2RS)-methylmalonyl-CoA 
• 18439-24-2 coenzyme A lithium salt 
• 110-15-6 succinic acid 
• 72-89-9 acetylcoenzyme 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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Novel coenzyme B12-dependent interconversion of isovaleryl-CoA and pivalyl-CoA

5′-Deoxyadenosylcobalamin (AdoCbl)-dependent isomerases catalyze carbon skeleton rearrangements using radical chemistry. We have recently characterized a fusion protein that comprises the two subunits of the AdoCbl-dependent isobutyryl- CoA mutase flanking a G-protein chaperone and named it isobutyryl-CoA mutase fused (IcmF). IcmF catalyzes the interconversion of isobutyryl-CoA and n-butyryl-CoA, whereas GTPase activity is associated with its G-protein domain. In this study, we report a novel activity associated with IcmF, i.e. the interconversion of isovaleryl-CoA and pivalyl-CoA. Kinetic characterization of IcmF yielded the following values: a Km for isovaleryl-CoA of 62 ± 8 μM and Vmax of 0.021 ± 0.004 μmol min-1 mg-1 at 37 ° C. Biochemical experiments show that an IcmF in which the base specificity loop motif NKXD is modified to NKXE catalyzes the hydrolysis of both GTP and ATP. IcmF is susceptible to rapid inactivation during turnover, and GTP conferred modest protection during utilization of isovaleryl-CoA as substrate. Interestingly, there was no protection from inactivation when either isobutyryl-CoA or n-butyryl-CoA was used as substrate. Detailed kinetic analysis indicated that inactivation is associated with loss of the 5′-deoxyadenosine moiety from the active site, precluding reformation of AdoCbl at the end of the turnover cycle. Under aerobic conditions, oxidation of the cob(II)alamin radical in the inactive enzyme results in accumulation of aquacobalamin. Because pivalic acid found in sludge can be used as a carbon source by some bacteria and isovaleryl- CoA is an intermediate in leucine catabolism, our discovery of a new isomerase activity associated with IcmF expands its metabolic potential.