Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates

William W. Farrar, Kent Plowman

Research output: Contribution to journal › Article

8 Citations (Scopus)

Abstract

The initial velocity, product inhibition, and isotopic exchange data show that the substrates of bovine heart mitochondrial acetyl-CoA synthetase add to the enzyme in an ordered fashion, with MgATP adding first followed by the addition of acetate, then the release of MgPPi immediately before the addition of CoA.

Original languageEnglish (US)
Pages (from-to)537-542
Number of pages6
JournalInternational Journal of Biochemistry
Volume6
Issue number8
DOIs
StatePublished - Jan 1 1975

Fingerprint

Acetate-CoA Ligase
Electronic data interchange
Coenzyme A
Acetates
Adenosine Triphosphate
Kinetics
Substrates
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates. / Farrar, William W.; Plowman, Kent.

In: International Journal of Biochemistry, Vol. 6, No. 8, 01.01.1975, p. 537-542.

Research output: Contribution to journal › Article

Farrar, WW & Plowman, K 1975, 'Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates', International Journal of Biochemistry, vol. 6, no. 8, pp. 537-542. https://doi.org/10.1016/0020-711X(75)90069-5
Farrar WW, Plowman K. Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates. International Journal of Biochemistry. 1975 Jan 1;6(8):537-542. https://doi.org/10.1016/0020-711X(75)90069-5
Farrar, William W. ; Plowman, Kent. / Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates. In: International Journal of Biochemistry. 1975 ; Vol. 6, No. 8. pp. 537-542.
@article{d8eb7fe0666c493b9d0aa62221ea0f65,
title = "Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates",
abstract = "The initial velocity, product inhibition, and isotopic exchange data show that the substrates of bovine heart mitochondrial acetyl-CoA synthetase add to the enzyme in an ordered fashion, with MgATP adding first followed by the addition of acetate, then the release of MgPPi immediately before the addition of CoA.",
author = "Farrar, {William W.} and Kent Plowman",
year = "1975",
month = "1",
day = "1",
doi = "10.1016/0020-711X(75)90069-5",
language = "English (US)",
volume = "6",
pages = "537--542",
journal = "International Journal of Biochemistry and Cell Biology",
issn = "1357-2725",
publisher = "Elsevier Limited",
number = "8",

}

TY - JOUR

T1 - Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates

AU - Farrar, William W.

AU - Plowman, Kent

PY - 1975/1/1

Y1 - 1975/1/1

N2 - The initial velocity, product inhibition, and isotopic exchange data show that the substrates of bovine heart mitochondrial acetyl-CoA synthetase add to the enzyme in an ordered fashion, with MgATP adding first followed by the addition of acetate, then the release of MgPPi immediately before the addition of CoA.

AB - The initial velocity, product inhibition, and isotopic exchange data show that the substrates of bovine heart mitochondrial acetyl-CoA synthetase add to the enzyme in an ordered fashion, with MgATP adding first followed by the addition of acetate, then the release of MgPPi immediately before the addition of CoA.

UR - http://www.scopus.com/inward/record.url?scp=32844454720&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=32844454720&partnerID=8YFLogxK

U2 - 10.1016/0020-711X(75)90069-5

DO - 10.1016/0020-711X(75)90069-5

M3 - Article

AN - SCOPUS:32844454720

VL - 6

SP - 537

EP - 542

JO - International Journal of Biochemistry and Cell Biology

JF - International Journal of Biochemistry and Cell Biology

SN - 1357-2725

IS - 8

ER -

Access to Document