Four Trypanosoma brucei fatty acyl-CoA synthetases: Fatty acid specificity of the recombinant proteins

D. W. Jiang; P. T. Englund

doi:10.1042/0264-6021:3580757

Four Trypanosoma brucei fatty acyl-CoA synthetases: Fatty acid specificity of the recombinant proteins

D. W. Jiang, P. T. Englund

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

12 Scopus citations

Abstract

As part of our investigation of fatty acid metabolism in Trypanosoma brucei, we have expressed four acyl-CoA synthetase (TbACS) genes in Esherichia coli. The recombinant proteins, with His-tags on their C-termini, were purified to near homogeneity using nickel-chelate affinity chromatography. Although these enzymes are highly homologous, they have distinct specificities for fatty acid chain length. TbACS1 prefers saturated fatty acids in the range C_11:0 to C_14:0 and TbACS2 prefers shorter fatty acids, mainly C_10:0. TbACS3 and 4, which have 95% sequence identity, have similar specificities, favouring fatty acids between C_14:0 and C_17:0. In addition, TbACS1, 3 and 4 function well with a variety of unsaturated fatty acids.

Original language	English (US)
Pages (from-to)	757-761
Number of pages	5
Journal	Biochemical Journal
Volume	358
Issue number	3
DOIs	https://doi.org/10.1042/0264-6021:3580757
State	Published - Sep 15 2001
Externally published	Yes

Keywords

ACS signature motif
Enzyme-coupled assay
Fatty acid chain length
Glycosyl phosphatidylinositol myristoylation
Recombinant acyl-CoA synthetases (ACS)

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1042/0264-6021:3580757

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title = "Four Trypanosoma brucei fatty acyl-CoA synthetases: Fatty acid specificity of the recombinant proteins",

abstract = "As part of our investigation of fatty acid metabolism in Trypanosoma brucei, we have expressed four acyl-CoA synthetase (TbACS) genes in Esherichia coli. The recombinant proteins, with His-tags on their C-termini, were purified to near homogeneity using nickel-chelate affinity chromatography. Although these enzymes are highly homologous, they have distinct specificities for fatty acid chain length. TbACS1 prefers saturated fatty acids in the range C11:0 to C14:0 and TbACS2 prefers shorter fatty acids, mainly C10:0. TbACS3 and 4, which have 95% sequence identity, have similar specificities, favouring fatty acids between C14:0 and C17:0. In addition, TbACS1, 3 and 4 function well with a variety of unsaturated fatty acids.",

keywords = "ACS signature motif, Enzyme-coupled assay, Fatty acid chain length, Glycosyl phosphatidylinositol myristoylation, Recombinant acyl-CoA synthetases (ACS)",

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AU - Englund, P. T.

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AB - As part of our investigation of fatty acid metabolism in Trypanosoma brucei, we have expressed four acyl-CoA synthetase (TbACS) genes in Esherichia coli. The recombinant proteins, with His-tags on their C-termini, were purified to near homogeneity using nickel-chelate affinity chromatography. Although these enzymes are highly homologous, they have distinct specificities for fatty acid chain length. TbACS1 prefers saturated fatty acids in the range C11:0 to C14:0 and TbACS2 prefers shorter fatty acids, mainly C10:0. TbACS3 and 4, which have 95% sequence identity, have similar specificities, favouring fatty acids between C14:0 and C17:0. In addition, TbACS1, 3 and 4 function well with a variety of unsaturated fatty acids.

KW - ACS signature motif

KW - Enzyme-coupled assay

KW - Fatty acid chain length

KW - Glycosyl phosphatidylinositol myristoylation

KW - Recombinant acyl-CoA synthetases (ACS)

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Four Trypanosoma brucei fatty acyl-CoA synthetases: Fatty acid specificity of the recombinant proteins

Abstract

Keywords

ASJC Scopus subject areas

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