Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase
Lipoic acid is a sulfur-containing 8-carbon fatty acid that functions as a central cofactor in multienzyme complexes that are involved in the oxidative decarboxylation of glycine and several α-keto acids. In its functional form, it is bound covalently in an amide linkage to the ε-amino group of a co...
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Published in | Protein expression and purification Vol. 39; no. 2; pp. 269 - 282 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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Elsevier Inc
01.02.2005
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Abstract | Lipoic acid is a sulfur-containing 8-carbon fatty acid that functions as a central cofactor in multienzyme complexes that are involved in the oxidative decarboxylation of glycine and several α-keto acids. In its functional form, it is bound covalently in an amide linkage to the ε-amino group of a conserved lysine residue of the “lipoyl bearing subunit,” resulting in a long “swinging arm” that shuttles intermediates among the requisite active sites. In
Escherichia coli and many other organisms, the lipoyl cofactor can be synthesized endogenously. The 8-carbon fatty-acyl chain is constructed via the type II fatty acid biosynthetic pathway as an appendage to the acyl carrier protein (ACP). Lipoyl(octanoyl)transferase (LipB) transfers the octanoyl chain from ACP to the target lysine acceptor, generating the substrate for lipoyl synthase (LS), which subsequently catalyzes insertion of both sulfur atoms into the C-6 and C-8 positions of the octanoyl chain. In this study, we present a three-step isolation procedure that results in a 14-fold purification of LipB to >95% homogeneity in an overall yield of 25%. We also show that the protein catalyzes the transfer of the octanoyl group from octanoyl-ACP to apo-H protein, which is the lipoyl bearing subunit of the glycine cleavage system. The specific activity of the purified protein is 0.541
U
mg
−1, indicating a turnover number of ∼0.2
s
−1, and the apparent
K
m values for octanoyl-ACP and apo-H protein are 10.2
±
4.4 and 13.2
±
2.9
μM, respectively. |
---|---|
AbstractList | Lipoic acid is a sulfur-containing 8-carbon fatty acid that functions as a central cofactor in multienzyme complexes that are involved in the oxidative decarboxylation of glycine and several alpha-keto acids. In its functional form, it is bound covalently in an amide linkage to the epsilon-amino group of a conserved lysine residue of the "lipoyl bearing subunit," resulting in a long "swinging arm" that shuttles intermediates among the requisite active sites. In Escherichia coli and many other organisms, the lipoyl cofactor can be synthesized endogenously. The 8-carbon fatty-acyl chain is constructed via the type II fatty acid biosynthetic pathway as an appendage to the acyl carrier protein (ACP). Lipoyl(octanoyl)transferase (LipB) transfers the octanoyl chain from ACP to the target lysine acceptor, generating the substrate for lipoyl synthase (LS), which subsequently catalyzes insertion of both sulfur atoms into the C-6 and C-8 positions of the octanoyl chain. In this study, we present a three-step isolation procedure that results in a 14-fold purification of LipB to >95% homogeneity in an overall yield of 25%. We also show that the protein catalyzes the transfer of the octanoyl group from octanoyl-ACP to apo-H protein, which is the lipoyl bearing subunit of the glycine cleavage system. The specific activity of the purified protein is 0.541 U mg(-1), indicating a turnover number of approximately 0.2 s(-1), and the apparent Km values for octanoyl-ACP and apo-H protein are 10.2+/-4.4 and 13.2+/-2.9 microM, respectively. Lipoic acid is a sulfur-containing 8-carbon fatty acid that functions as a central cofactor in multienzyme complexes that are involved in the oxidative decarboxylation of glycine and several alpha-keto acids. In its functional form, it is bound covalently in an amide linkage to the epsilon-amino group of a conserved lysine residue of the "lipoyl bearing subunit," resulting in a long "swinging arm" that shuttles intermediates among the requisite active sites. In Escherichia coli and many other organisms, the lipoyl cofactor can be synthesized endogenously. The 8-carbon fatty-acyl chain is constructed via the type II fatty acid biosynthetic pathway as an appendage to the acyl carrier protein (ACP). Lipoyl(octanoyl)transferase (LipB) transfers the octanoyl chain from ACP to the target lysine acceptor, generating the substrate for lipoyl synthase (LS), which subsequently catalyzes insertion of both sulfur atoms into the C-6 and C-8 positions of the octanoyl chain. In this study, we present a three-step isolation procedure that results in a 14-fold purification of LipB to >95% homogeneity in an overall yield of 25%. We also show that the protein catalyzes the transfer of the octanoyl group from octanoyl-ACP to apo-H protein, which is the lipoyl bearing subunit of the glycine cleavage system. The specific activity of the purified protein is 0.541 U mg(-1), indicating a turnover number of approximately 0.2 s(-1), and the apparent Km values for octanoyl-ACP and apo-H protein are 10.2+/-4.4 and 13.2+/-2.9 microM, respectively. Lipoic acid is a sulfur-containing 8-carbon fatty acid that functions as a central cofactor in multienzyme complexes that are involved in the oxidative decarboxylation of glycine and several α-keto acids. In its functional form, it is bound covalently in an amide linkage to the ε-amino group of a conserved lysine residue of the “lipoyl bearing subunit,” resulting in a long “swinging arm” that shuttles intermediates among the requisite active sites. In Escherichia coli and many other organisms, the lipoyl cofactor can be synthesized endogenously. The 8-carbon fatty-acyl chain is constructed via the type II fatty acid biosynthetic pathway as an appendage to the acyl carrier protein (ACP). Lipoyl(octanoyl)transferase (LipB) transfers the octanoyl chain from ACP to the target lysine acceptor, generating the substrate for lipoyl synthase (LS), which subsequently catalyzes insertion of both sulfur atoms into the C-6 and C-8 positions of the octanoyl chain. In this study, we present a three-step isolation procedure that results in a 14-fold purification of LipB to >95% homogeneity in an overall yield of 25%. We also show that the protein catalyzes the transfer of the octanoyl group from octanoyl-ACP to apo-H protein, which is the lipoyl bearing subunit of the glycine cleavage system. The specific activity of the purified protein is 0.541 U mg −1, indicating a turnover number of ∼0.2 s −1, and the apparent K m values for octanoyl-ACP and apo-H protein are 10.2 ± 4.4 and 13.2 ± 2.9 μM, respectively. |
Author | Goodson, Kathy Baleanu-Gogonea, Camelia Fox, Brian G. Broadwater, John A. Iwig, David F. Cicchillo, Robert M. Haas, Jeffrey A. Nesbitt, Natasha M. Booker, Squire J. |
Author_xml | – sequence: 1 givenname: Natasha M. surname: Nesbitt fullname: Nesbitt, Natasha M. organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA – sequence: 2 givenname: Camelia surname: Baleanu-Gogonea fullname: Baleanu-Gogonea, Camelia organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA – sequence: 3 givenname: Robert M. surname: Cicchillo fullname: Cicchillo, Robert M. organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA – sequence: 4 givenname: Kathy surname: Goodson fullname: Goodson, Kathy organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA – sequence: 5 givenname: David F. surname: Iwig fullname: Iwig, David F. organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA – sequence: 6 givenname: John A. surname: Broadwater fullname: Broadwater, John A. organization: Department of Biochemistry, The University of Wisconsin–Madison, Madison, WI 53706, USA – sequence: 7 givenname: Jeffrey A. surname: Haas fullname: Haas, Jeffrey A. organization: Department of Biochemistry, The University of Wisconsin–Madison, Madison, WI 53706, USA – sequence: 8 givenname: Brian G. surname: Fox fullname: Fox, Brian G. organization: Department of Biochemistry, The University of Wisconsin–Madison, Madison, WI 53706, USA – sequence: 9 givenname: Squire J. surname: Booker fullname: Booker, Squire J. email: sjb14@psu.edu organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA |
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Keywords | Lipoyl synthase Lipoic acid H protein Lipoyl transferase Fatty acid biosynthesis Acyl carrier protein Octanoyl-ACP LipA LipB Glycine cleavage system |
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SubjectTerms | Acyl carrier protein Acyl Carrier Protein - metabolism Acyltransferases - genetics Acyltransferases - isolation & purification Acyltransferases - metabolism Amino Acid Oxidoreductases Apoproteins - metabolism Carrier Proteins Chromatography, Gel Chromatography, High Pressure Liquid Cloning, Molecular Electrophoresis, Polyacrylamide Gel Escherichia coli - enzymology Escherichia coli Proteins - genetics Escherichia coli Proteins - isolation & purification Escherichia coli Proteins - metabolism Fatty acid biosynthesis Gene Expression Glycine cleavage system H protein Histidine - chemistry Hydrogen-Ion Concentration Isoelectric Point Kinetics LipA LipB Lipoic acid Lipoyl synthase Lipoyl transferase Models, Biological Molecular Weight Multienzyme Complexes Octanoyl-ACP Osmolar Concentration Plasmids Polymerase Chain Reaction Protein Structure, Quaternary Spectrometry, Mass, Electrospray Ionization Transferases |
Title | Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase |
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