Definition by functional and structural analysis of two malonyl-CoA sites in carnitine palmitoyltransferase 1A (Q28298983)

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29 December 2019

title

Definition by functional and structural analysis of two malonyl-CoA sites in carnitine palmitoyltransferase 1A (English)

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29 December 2019

4

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Dolors Serra Cucurull

6

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29 December 2019

Paulino Gómez-Puertas

9

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author name string

Eduardo López-Viñas

1

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29 December 2019

Assia Bentebibel

2

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29 December 2019

Chandrashekaran Gurunathan

3

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29 December 2019

Dolores de Arriaga

5

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Guillermina Asins

7

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Fausto G Hegardt

8

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language of work or name

English

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publication date

23 April 2007

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Journal of Biological Chemistry

29 December 2019

published in

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29 December 2019

volume

282

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issue

25

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page(s)

18212-18224

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The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis

29 December 2019

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High expression of a novel carnitine palmitoyltransferase I like protein in rat brown adipose tissue and heart: isolation and characterization of its cDNA clone

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A novel brain-expressed protein related to carnitine palmitoyltransferase I

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Hypothalamic malonyl-CoA triggers mitochondrial biogenesis and oxidative gene expression in skeletal muscle: Role of PGC-1alpha.

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Changes in the ability of malonyl-CoA to inhibit carnitine palmitoyltransferase I activity and to bind to rat liver mitochondria during incubation in vitro. Differences in binding at 0 degree C and 37 degrees C with a fixed concentration of malonyl-

21 January 2018

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Time-dependence of inhibition of carnitine palmitoyltransferase I by malonyl-CoA in mitochondria isolated from livers of fed or starved rats. Evidence for transition of the enzyme between states of low and high affinity for malonyl-CoA.

21 January 2018

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Binding of malonyl-CoA to isolated mitochondria. Evidence for high- and low-affinity sites in liver and heart and relationship to inhibition of carnitine palmitoyltransferase activity

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Interacting effects of L-carnitine and malonyl-CoA on rat liver carnitine palmitoyltransferase

21 January 2018

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The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding

21 January 2018

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Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for malonyl-CoA inhibition. Mutation of methionine 593 abolishes malonyl-CoA inhibition

21 January 2018

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Specificity of the interactions between Glu-3, Ser-24, and Gln-30 within the N-terminal segment of rat liver mitochondrial overt carnitine palmitoyltransferase (L-CPT I) in determining the malonyl-CoA sensitivity of the enzyme

21 January 2018

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Demonstration of N- and C-terminal domain intramolecular interactions in rat liver carnitine palmitoyltransferase 1 that determine its degree of malonyl-CoA sensitivity

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The mitochondrial intermembrane loop region of rat carnitine palmitoyltransferase 1A is a major determinant of its malonyl-CoA sensitivity

21 January 2018

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Role of carnitine in hepatic ketogenesis

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Effects of fasting, adrenalectomy and streptozotocin-diabetes on sensitivity of hepatic carnitine acyltransferase to malonyl CoA.

21 January 2018

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Observations on the affinity for carnitine, and malonyl-CoA sensitivity, of carnitine palmitoyltransferase I in animal and human tissues. Demonstration of the presence of malonyl-CoA in non-hepatic tissues of the rat

21 January 2018

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Effects of pH on the interaction of substrates and malonyl-CoA with mitochondrial carnitine palmitoyltransferase I.

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Structural model of the catalytic core of carnitine palmitoyltransferase I and carnitine octanoyltransferase (COT): mutation of CPT I histidine 473 and alanine 381 and COT alanine 238 impairs the catalytic activity

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M700885200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17452323%20AND%20SRC:MED&resulttype=core&format=json

29 December 2019

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