Affinity chromatography and affinity labeling of rat liver succinyl-CoA synthetase.

Ball, Dorothy J.; Nishimura, Jonathan S.

doi:10.1016/s0021-9258(19)70379-2

Cited by 15 publications

(1 citation statement)

References 39 publications

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“…Since the isolated a subunit (Pearson & Bridger, 1975a) is capable of being phosphorylated by ATP, it is reasonable to conclude that the nucleoside diand triphosphate binding site, or part of it, is located on the a subunit (Pearson & Bridger, 1975b). Evidence consistent with participation of both subunits in the composition of this site has been presented recently (Ball & Nishimura, 1980). Indeed, Pearson Bridger (1975b) have demonstrated a dramatic enhancement of ATP phosphorylation of the isolated a subunit when the ß subunit is added.…”

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confidence: 93%

Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-CoA synthetase from Escherichia coli

Prasad¹,

Nishimura²,

Horowitz³

1982

Biochemistry

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confidence: 93%

Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-CoA synthetase from Escherichia coli

Prasad¹,

Nishimura²,

Horowitz³

1982

Biochemistry

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Succinyl‐CoA Synthetase Structure‐Function Relationships and Other Considerations

Nishimura

1986

Advances in Enzymology - And Related Areas of Molecular Biology

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Regulatory role of GDP in the phosphoenzyme formation of guanine nucleotide: Specific forms of succinyl coenzyme a synthetase

Klein

1994

J Protein Chem

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We have previously shown that micromolar concentrations of GDP stimulate the GTP-mediated phosphorylation of p36, the alpha subunit of succinyl-CoA synthetase (SCS), in lysates prepared from Dictyostelium discoideum. In this study, we report that this phenomenon represents an enhanced catalytic capacity of SCS to form the phosphoenzyme intermediate. Low concentrations of GDP stimulate phosphoenzyme formation by either GTP, or succinyl-CoA and P(i). Under these conditions GDP enhances the apparent rate of phosphoenzyme formation but does not significantly alter the fraction of phosphorylated enzyme. This effect is retained during purification of the protein and is also observed with purified pig heart SCS, indicating that GDP directly alters the enzyme to enhance its rate of phosphorylation. Under these conditions, GDP does not function at the catalytic site, implying an allosteric regulation of SCS.

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Affinity chromatography and affinity labeling of rat liver succinyl-CoA synthetase.

Cited by 15 publications

References 39 publications

Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-CoA synthetase from Escherichia coli

Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-CoA synthetase from Escherichia coli

Succinyl‐CoA Synthetase Structure‐Function Relationships and Other Considerations

Regulatory role of GDP in the phosphoenzyme formation of guanine nucleotide: Specific forms of succinyl coenzyme a synthetase

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