Literature DB >> 6335031

Purification and some kinetic properties of rat liver ATP citrate lyase.

B Houston, H G Nimmo.   

Abstract

A new purification procedure for rat liver ATP citrate lyase is described. The method reproducibly gives homogenous undegraded enzyme. Steady-state kinetic analysis of ATP citrate lyase was complicated by the presence of ADP, a product of the reaction, in solutions of ATP. The kinetic patterns observed were dependent on whether ADP was removed by the assay system. When assays were performed with a method in which ADP was removed, the results showed that the enzyme obeys a double-displacement mechanism with a phosphoenzyme intermediate. This resolves a controversy between the results of previous kinetic studies and those of isotope-exchange and enzyme-labelling experiments.

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Year:  1984        PMID： 6335031      PMCID： PMC1144450          DOI： 10.1042/bj2240437

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  28 in total

1.  ATP-citrate lyase kinase and cyclic AMP-dependent protein kinase phosphorylate different sites on ATP-citrate lyase.

Authors:  S Ramakrishna; D L Pucci; W B Benjamin
Journal:  J Biol Chem       Date:  1981-10-25       Impact factor: 5.157

2.  Purification and physicochemical properties of ATP citrate (pro-3S) lyase from lactating rat mammary gland and studies of its reversible phosphorylation.

Authors:  P S Guy; P Cohen; D G Hardie
Journal:  Eur J Biochem       Date:  1981-02

3.  Dependence of ATP-citrate lyase kinase activity on the phosphorylation of ATP-citrate lyase by cyclic AMP-dependent protein kinase.

Authors:  S Ramakrishna; D L Pucci; W B Benjamin
Journal:  J Biol Chem       Date:  1983-04-25       Impact factor: 5.157

4.  Rat mammary gland ATP-citrate lyase is phosphorylated by cyclic amp-dependent protein kinase.

Authors:  P S Guy; P Cohen; D G Hardie
Journal:  FEBS Lett       Date:  1980-01-14       Impact factor: 4.124

5.  A rapid purification of hepatic ATP citrate lyase using blue Sepharose.

Authors:  J C Redshaw; E G Loten
Journal:  FEBS Lett       Date:  1981-01-26       Impact factor: 4.124

6.  Fat cell protein phosphorylation. Identification of phosphoprotein-2 as ATP-citrate lyase.

Authors:  S Ramakrishna; W B Benjamin
Journal:  J Biol Chem       Date:  1979-09-25       Impact factor: 5.157

7.  Phosphorylation of ATP citrate lyase in response to glucagon.

Authors:  A M Janski; P A Srere; N W Cornell; R L Veech
Journal:  J Biol Chem       Date:  1979-10-10       Impact factor: 5.157

8.  Acetyl coenzyme A carboxylase. Rapid purification of the chick liver enzyme and steady state kinetic analysis of the carboxylase-catalyzed reaction.

Authors:  N B Beaty; M D Lane
Journal:  J Biol Chem       Date:  1982-01-25       Impact factor: 5.157

9.  Influence of polyethylene glycols on the kinetics of rat liver phosphofructokinase.

Authors:  G D Reinhart
Journal:  J Biol Chem       Date:  1980-11-25       Impact factor: 5.157

10.  The interaction of fructose 2,6-bisphosphate with an allosteric site of rat liver fructose 1,6-bisphosphatase.

Authors:  D W Meek; H G Nimmo
Journal:  FEBS Lett       Date:  1983-08-22       Impact factor: 4.124
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  2 in total

1.  Citrate modulates lipopolysaccharide-induced monocyte inflammatory responses.

Authors:  M J Ashbrook; K L McDonough; J J Pituch; P L Christopherson; T T Cornell; D T Selewski; T P Shanley; N B Blatt
Journal:  Clin Exp Immunol       Date:  2015-04-19       Impact factor: 4.330

2.  Fatty acid chain elongation in palmitate-perfused working rat heart: mitochondrial acetyl-CoA is the source of two-carbon units for chain elongation.

Authors:  Janos Kerner; Paul E Minkler; Edward J Lesnefsky; Charles L Hoppel
Journal:  J Biol Chem       Date:  2014-02-20       Impact factor: 5.157
  2 in total

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