The mechanism of the succinic thiokinase reaction. Effector role of desulfo-coenzyme A in succinyl phosphate formation

Frederick Lawrence Grinnell, Jonathan S. Nishimura

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Incubation of highly purified Escherichia coli succinic thiokinase (succinate: coenzyme A ligase (adenosine diphosphate), EC 6.2.1.5) and the coenzyme A analog, desulfo-coenzyme A, with succinate, adenosine triphosphate, and Mg2+ resulted in stimulation of succinyl phosphate synthesis. This suggests that coenzyme A is required for optimal formation of enzyme-bound succinyl phosphate. The Km of desulfo-coenzyme A in this reaction was 6.2 × 10-5 M. A virtually absent ATPase activity of the enzyme was significantly stimulated by both coenzyme A and desulfo-coenzyme A. The Km of desulfo-coenzyme A in this reaction was 1.4 × 10-3 M. The possible significance of these results is discussed. During these studies it was found that succinyl phosphate is converted nonenzymatically into succinamic acid in the presence of (NH4)2SO4 at pH 7.2.

Original languageEnglish (US)
Pages (from-to)568-574
Number of pages7
JournalBiochemistry
Volume8
Issue number2
StatePublished - 1969

Fingerprint

Succinate-CoA Ligases
Coenzyme A
Succinic Acid
Coenzyme A Ligases
Enzymes
Adenosine Diphosphate
Escherichia coli
Adenosine Triphosphatases
Adenosine Triphosphate
Acids
desulfo-coenzyme A
succinyl phosphate

ASJC Scopus subject areas

  • Biochemistry

Cite this

The mechanism of the succinic thiokinase reaction. Effector role of desulfo-coenzyme A in succinyl phosphate formation. / Grinnell, Frederick Lawrence; Nishimura, Jonathan S.

In: Biochemistry, Vol. 8, No. 2, 1969, p. 568-574.

Research output: Contribution to journalArticle

@article{1586b102819f41b1a38123e5fdf17d30,
title = "The mechanism of the succinic thiokinase reaction. Effector role of desulfo-coenzyme A in succinyl phosphate formation",
abstract = "Incubation of highly purified Escherichia coli succinic thiokinase (succinate: coenzyme A ligase (adenosine diphosphate), EC 6.2.1.5) and the coenzyme A analog, desulfo-coenzyme A, with succinate, adenosine triphosphate, and Mg2+ resulted in stimulation of succinyl phosphate synthesis. This suggests that coenzyme A is required for optimal formation of enzyme-bound succinyl phosphate. The Km of desulfo-coenzyme A in this reaction was 6.2 × 10-5 M. A virtually absent ATPase activity of the enzyme was significantly stimulated by both coenzyme A and desulfo-coenzyme A. The Km of desulfo-coenzyme A in this reaction was 1.4 × 10-3 M. The possible significance of these results is discussed. During these studies it was found that succinyl phosphate is converted nonenzymatically into succinamic acid in the presence of (NH4)2SO4 at pH 7.2.",
author = "Grinnell, {Frederick Lawrence} and Nishimura, {Jonathan S.}",
year = "1969",
language = "English (US)",
volume = "8",
pages = "568--574",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "2",

}

TY - JOUR

T1 - The mechanism of the succinic thiokinase reaction. Effector role of desulfo-coenzyme A in succinyl phosphate formation

AU - Grinnell, Frederick Lawrence

AU - Nishimura, Jonathan S.

PY - 1969

Y1 - 1969

N2 - Incubation of highly purified Escherichia coli succinic thiokinase (succinate: coenzyme A ligase (adenosine diphosphate), EC 6.2.1.5) and the coenzyme A analog, desulfo-coenzyme A, with succinate, adenosine triphosphate, and Mg2+ resulted in stimulation of succinyl phosphate synthesis. This suggests that coenzyme A is required for optimal formation of enzyme-bound succinyl phosphate. The Km of desulfo-coenzyme A in this reaction was 6.2 × 10-5 M. A virtually absent ATPase activity of the enzyme was significantly stimulated by both coenzyme A and desulfo-coenzyme A. The Km of desulfo-coenzyme A in this reaction was 1.4 × 10-3 M. The possible significance of these results is discussed. During these studies it was found that succinyl phosphate is converted nonenzymatically into succinamic acid in the presence of (NH4)2SO4 at pH 7.2.

AB - Incubation of highly purified Escherichia coli succinic thiokinase (succinate: coenzyme A ligase (adenosine diphosphate), EC 6.2.1.5) and the coenzyme A analog, desulfo-coenzyme A, with succinate, adenosine triphosphate, and Mg2+ resulted in stimulation of succinyl phosphate synthesis. This suggests that coenzyme A is required for optimal formation of enzyme-bound succinyl phosphate. The Km of desulfo-coenzyme A in this reaction was 6.2 × 10-5 M. A virtually absent ATPase activity of the enzyme was significantly stimulated by both coenzyme A and desulfo-coenzyme A. The Km of desulfo-coenzyme A in this reaction was 1.4 × 10-3 M. The possible significance of these results is discussed. During these studies it was found that succinyl phosphate is converted nonenzymatically into succinamic acid in the presence of (NH4)2SO4 at pH 7.2.

UR - http://www.scopus.com/inward/record.url?scp=0014472726&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0014472726&partnerID=8YFLogxK

M3 - Article

C2 - 4240088

AN - SCOPUS:0014472726

VL - 8

SP - 568

EP - 574

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 2

ER -