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

William W. Farrar; Kent Plowman

doi:10.1016/0020-711X(75)90069-5

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

William W. Farrar, Kent Plowman

Physiological and Technological Nursing

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

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 language	English (US)
Pages (from-to)	537-542
Number of pages	6
Journal	International Journal of Biochemistry
Volume	6
Issue number	8
DOIs	https://doi.org/10.1016/0020-711X(75)90069-5
State	Published - Jan 1 1975

ASJC Scopus subject areas

Biochemistry

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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.",

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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.

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