A malonyl-CoA-binding protein from liver.

Abstract:

:A soluble protein that binds malonyl-CoA without requiring cofactors has been purified from rat liver. Until saturated, it competes with fatty acid synthetase for free malonyl-CoA, temporarily reducing the rate of fatty acid synthesis at low levels of malonyl-CoA, as in fatty acid synthetase--coupled assays for acetyl-CoA carboxylase. These assays yield low estimates for carboxylase activity with crude and partially purified homogenates containing the malonyl-CoA-binding protein. The protein does not inhibit assays for carboxylase activity that measure nonvolatile radioactivity incorporated from bicarbonate or NADH oxidation coupled to ADP formation. It has an Mr of 180,000 and a subunit of 90,000. It has a lower affinity for ATP, ADP, and acetyl-CoA and none for CO2 or fatty acid synthetase. No enzymatic function has been identified. The protein may regulate malonyl-CoA-binding enzymes.

authors

Dugan RE,Osterlund BR,Drong RF,Swenson TL

doi

10.1016/s0006-291x(87)80111-0

subject

Has Abstract

pub_date

1987-08-31 00:00:00

pages

234-41

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(87)80111-0

journal_volume

147

pub_type

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