Cysteine-scanning mutagenesis of muscle carnitine palmitoyltransferase I reveals a single cysteine residue (Cys-305) is important for catalysis (Q28296650)

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English	Cysteine-scanning mutagenesis of muscle carnitine palmitoyltransferase I reveals a single cysteine residue (Cys-305) is important for catalysis	scientific article

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scholarly article

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Cysteine-scanning mutagenesis of muscle carnitine palmitoyltransferase I reveals a single cysteine residue (Cys-305) is important for catalysis (English)

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author name string

Hongyan Liu

1

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Guolu Zheng

2

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Michelle Treber

3

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Jia Dai

4

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Gebre Woldegiorgis

5

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language of work or name

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publication date

11 February 2005

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Journal of Biological Chemistry

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280

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6

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4524-31

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1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400893200

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The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis

1 reference

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Functional studies of yeast-expressed human heart muscle carnitine palmitoyltransferase I.

1 reference

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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

1 reference

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Isolation and characterization of cDNA and genomic clones encoding human muscle type carnitine palmitoyltransferase I.

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Are the beta-cell signaling molecules malonyl-CoA and cystolic long-chain acyl-CoA implicated in multiple tissue defects of obesity and NIDDM?

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Acetyl-CoA carboxylase 2 mutant mice are protected against obesity and diabetes induced by high-fat/high-carbohydrate diets

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Functional characterization of mitochondrial carnitine palmitoyltransferases I and II expressed in the yeast Pichia pastoris

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Deletion of the conserved first 18 N-terminal amino acid residues in rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA sensitivity and binding.

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Substitution of glutamate-3, valine-19, leucine-23, and serine-24 with alanine in the N-terminal region of human heart muscle carnitine palmitoyltransferase I abolishes malonyl CoA inhibition and binding

1 reference

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21 January 2018

Leucine-764 near the extreme C-terminal end of carnitine palmitoyltransferase I is important for activity

1 reference

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Carnitine palmitoyltransferase. Activation by palmitoyl-CoA and inactivation by malonyl-CoA.

1 reference

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Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat liver carnitine palmitoyltransferase I that are important for catalytic activity and malonyl-CoA sensitivity

1 reference

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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

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Molecular basis of hepatic carnitine palmitoyltransferase I deficiency

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Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport

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Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase

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The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine

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The peroxisome proliferator-induced cytosolic type I acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid alpha /beta hydrolase

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21 January 2018

Lecithin retinol acyltransferase contains cysteine residues essential for catalysis

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Replacement of catalytic histidine-195 of chloramphenicol acetyltransferase: evidence for a general base role for glutamate

1 reference

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Identification by mutagenesis of a conserved glutamate (Glu487) residue important for catalytic activity in rat liver carnitine palmitoyltransferase II

1 reference

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Acyl-CoA synthetase isoforms 1, 4, and 5 are present in different subcellular membranes in rat liver and can be inhibited independently

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21 January 2018

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10.1074/JBC.M400893200

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