Investigation of the solution conformation of coenzyme A and its derivatives by hydrogen-1 and phosphorus-31 fast Fourier transform nuclear magnetic resonance spectroscopy

Lee, Che-Hung; Sarma, Ramaswamy H.

doi:10.1021/ja00838a043

Cited by 53 publications

(11 citation statements)

References 11 publications

(11 reference statements)

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“…The measured coupling constants correspond to a population distribution of 72% trans and 14% each of the two gauche conformations between the β-phosphorus and the C2‘‘ carbon. This result is in agreement with previous studies of CoA and CoA derivatives. , …”

Section: Resultssupporting

confidence: 94%

“…Despite its importance, there have been surprisingly few detailed NMR studies of CoA or CoA derivatives. Early work used classical one-dimensional (1D) methods to assign the proton − and carbon , NMR spectra. More recently, Anderson and co-workers used two-dimensional (2D) experiments in conjunction with 1D 1 H NOE difference experiments to assign the proton and carbon spectra of CoA .…”

Section: Introductionmentioning

confidence: 99%

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Stereospecific ¹H and ¹³C NMR Assignments of Crotonyl CoA and Hexadienoyl CoA: Conformational Analysis and Comparison with Protein−CoA Complexes

Tonge

Raleigh

1998

J. Am. Chem. Soc.

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Stereospecific 1 H and 13 C resonance assignments of hexadienoyl-CoA and crotonyl-CoA have been determined. The two diastereotopic methyl groups at the C2′′ carbon were assigned via transferred nuclear Overhauser effect experiments on the complex of hexadienoyl-CoA with the enzyme enoyl-CoA hydratase. The two diastereotopic 1′′ protons were assigned using heteronuclear multiple-bond correlation experiments in conjunction with rotating frame nuclear Overhauser spectroscopy. This represents the first set of complete stereospecific assignments for any CoA derivative. The assignments allow a detailed quantitative conformational analysis of the uncomplexed form of the molecule. In particular, the relative population of the various rotamers about the C1′′-C2′′ and the C2′′-C3′′ bonds have been determined. The database of protein-bound CoA structures has been surveyed and used to compare the structure(s) of CoA in protein-CoA complexes with the conformational preferences of free CoA.

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Section: Resultssupporting

confidence: 94%

Section: Introductionmentioning

confidence: 99%

Stereospecific ¹H and ¹³C NMR Assignments of Crotonyl CoA and Hexadienoyl CoA: Conformational Analysis and Comparison with Protein−CoA Complexes

Tonge

Raleigh

1998

J. Am. Chem. Soc.

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“…The more dynamic behavior of CoA is, in some sense, to be completely expected given its flexibility. As outlined in the Introduction, it is known from the crystal structure that CoA bridges two units of the PFL and, thus, prefers the syn conformation, whereas the anti conformation is dominant in its unbound state (Figure a) …”

Section: Resultsmentioning

confidence: 99%

“…Further, it is found that CoA binds close to the interface between two subunits in the dimer, with one CoA bound to the surface of each subunit and approximately 30 Å from the active site . Bound CoA adopts the unusual syn conformation with respect to the N‐glycosidic bond, although the anti arrangement is the preferred conformation of free CoA in solution . In the syn conformation, the thiol group on the pantothenate chain is located in the predominantly hydrophobic pocket formed by the side chains of residues F200 and H227 of the opposing monomer.…”

Section: Introductionmentioning

confidence: 99%

The Influence of Chemical Change on Protein Dynamics: A Case Study with Pyruvate Formate‐Lyase

Hanževački¹,

Čondić‐Jurkić

Banhatti

et al. 2019

Chemistry A European J

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What is the most significant result of this study?The mechanism of pyruvate formate-lyase plays ak ey role in the anaerobic glucose metabolism of E. coli and other microbes, catalysing the breakdown of pyruvate and the subsequent acetylation of coenzyme A( CoA), via an acetylated protein intermediate, in two half-reactions. Using extensive molecular dynamics simulations, we have highlighted the impact of acetylation of the active site of the enzyme during the first half-reaction. This minor chemical change, on al ength scale of ac ouple of ngstroms, causes a change in the fluctuation spectrum of the entire enzymatic system, revealing ap otential channel for CoA, which is initially bound to the protein surface, to enter into the buried active site in order to trigger the second half-reaction.

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“…An easy explanation would be that there is some structural feature of coenzyme A, caused by hydrogen bonding or another factor, which requires these components. NMR studies show an extended conformation for the most part in aqueous solution (Lee and Sarma 1975;Mieyal et al 1976;Roeder et al 1975) although molecular orbital studies indicate a few stable hydrogen bonds (Perahia and Cebe 1977).…”

Section: Discussionmentioning

confidence: 99%

Prebiotic syntheses of vitamin coenzymes: II. Pantoic acid, pantothenic acid, and the composition of coenzyme A

Miller

Schlesinger

1993

J Mol Evol

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Pantoic acid can by synthesized in good prebiotic yield from isobutyraldehyde or et-ketoisovaleric acid + H2CO + HCN. Isobutyraldehyde is the Strecker precursor to valine and a-ketoisovaleric acid is the valine transamination product. Mg z+ and Ca 2+ as well as several transition metals are catalysts for the a-ketoisovaleric acid reaction. Pantothenic acid is produced from pantoyl lactone (easily formed from pantoic acid) and the relatively high concentrations of I~-alanine that would be formed on drying prebiotic amino acid mixtures. There is no selectivity for this reaction over glycine, alanine, or ~/-amino butyric acid. The components of coenzyme A are discussed in terms of ease of prebiotic formation and stability and are shown to be plausible choices, but many other compounds are possible. The ~/-OH of pantoic acid needs to be capped to prevent decomposition of pantothenic acid. These results suggest that coenzyme A function was important in the earliest metabolic pathways and that the coenzyme A precursor contained most of the components of the present coenzyme.

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Investigation of the solution conformation of coenzyme A and its derivatives by hydrogen-1 and phosphorus-31 fast Fourier transform nuclear magnetic resonance spectroscopy

Cited by 53 publications

References 11 publications

Stereospecific ¹H and ¹³C NMR Assignments of Crotonyl CoA and Hexadienoyl CoA: Conformational Analysis and Comparison with Protein−CoA Complexes

Stereospecific ¹H and ¹³C NMR Assignments of Crotonyl CoA and Hexadienoyl CoA: Conformational Analysis and Comparison with Protein−CoA Complexes

The Influence of Chemical Change on Protein Dynamics: A Case Study with Pyruvate Formate‐Lyase

Prebiotic syntheses of vitamin coenzymes: II. Pantoic acid, pantothenic acid, and the composition of coenzyme A

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Investigation of the solution conformation of coenzyme A and its derivatives by hydrogen-1 and phosphorus-31 fast Fourier transform nuclear magnetic resonance spectroscopy

Cited by 53 publications

References 11 publications

Stereospecific 1H and 13C NMR Assignments of Crotonyl CoA and Hexadienoyl CoA: Conformational Analysis and Comparison with Protein−CoA Complexes

Stereospecific 1H and 13C NMR Assignments of Crotonyl CoA and Hexadienoyl CoA: Conformational Analysis and Comparison with Protein−CoA Complexes

The Influence of Chemical Change on Protein Dynamics: A Case Study with Pyruvate Formate‐Lyase

Prebiotic syntheses of vitamin coenzymes: II. Pantoic acid, pantothenic acid, and the composition of coenzyme A

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Stereospecific ¹H and ¹³C NMR Assignments of Crotonyl CoA and Hexadienoyl CoA: Conformational Analysis and Comparison with Protein−CoA Complexes

Stereospecific ¹H and ¹³C NMR Assignments of Crotonyl CoA and Hexadienoyl CoA: Conformational Analysis and Comparison with Protein−CoA Complexes