Biotin: Biogenesis, Transport, and Their Regulation

Eisenberg, Max A.

doi:10.1002/9780470122839.ch7

Cited by 29 publications

(8 citation statements)

References 127 publications

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“…Structural relationships have long been postulated to exist between different members of this group. [28][29][30] In particular, a clear similarity has been demonstrated between the active sites of BirA and class II aminoacyl-tRNA synthases. 31 When the cofactor-binding sites of the E. coli BirA 18 and T. acidophilum LplA are superimposed, it can be seen that a lysine residue (Lys145 in T. acidophilum numbering) that is conserved in the primary structures of all biotin and lipoate protein ligases is located in exactly the same position and orientation in the two structures, thus underlining its importance (Figure 4(a) and (b)).…”

Section: Comparison Of T Acidophilum Lpla With E Coli Bira Implicatmentioning

confidence: 95%

Structure of a Putative Lipoate Protein Ligase from Thermoplasma acidophilum and the Mechanism of Target Selection for Post-translational Modification

McManus

Luisi

Perham

2006

Journal of Molecular Biology

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Lipoyl-lysine swinging arms are crucial to the reactions catalysed by the 2-oxo acid dehydrogenase multienzyme complexes. A gene encoding a putative lipoate protein ligase (LplA) of Thermoplasma acidophilum was cloned and expressed in Escherichia coli. The recombinant protein, a monomer of molecular mass 29 kDa, was catalytically inactive. Crystal structures in the absence and presence of bound lipoic acid were solved at 2.1 A resolution. The protein was found to fall into the alpha/beta class and to be structurally homologous to the catalytic domains of class II aminoacyl-tRNA synthases and biotin protein ligase, BirA. Lipoic acid in LplA was bound in the same position as biotin in BirA. The structure of the T.acidophilum LplA and limited proteolysis of E.coli LplA together highlighted some key features of the post-translational modification. A loop comprising residues 71-79 in the T.acidophilum ligase is proposed as interacting with the dithiolane ring of lipoic acid and discriminating against the entry of biotin. A second loop comprising residues 179-193 was disordered in the T.acidophilum structure; tryptic cleavage of the corresponding loop in the E.coli LplA under non-denaturing conditions rendered the enzyme catalytically inactive, emphasizing its importance. The putative LplA of T.acidophilum lacks a C-terminal domain found in its counterparts in E.coli (Gram-negative) or Streptococcus pneumoniae (Gram-positive). A gene encoding a protein that appears to have structural homology to the additional domain in the E.coli and S.pneumoniae enzymes was detected alongside the structural gene encoding the putative LplA in the T.acidophilum genome. It is likely that this protein is required to confer activity on the LplA as currently purified, one protein perhaps catalysing the formation of the obligatory lipoyl-AMP intermediate, and the other transferring the lipoyl group from it to the specific lysine residue in the target protein.

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Section: Comparison Of T Acidophilum Lpla With E Coli Bira Implicatmentioning

confidence: 95%

Structure of a Putative Lipoate Protein Ligase from Thermoplasma acidophilum and the Mechanism of Target Selection for Post-translational Modification

McManus

Luisi

Perham

2006

Journal of Molecular Biology

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“…Vitamin H (biotin) is essential for all living cells, where it serves as a mobile carrier of activated CO 2 (Dakshinamurti et al ., 1985; Knowles, 1989). Plants can synthesize their own biotin (Baldet et al ., 1993; Baldet et al ., 1997), and the biosynthetic pathway appears to be identical to that described for bacteria (Eisenberg, 1973; Pai, 1975). To date, four biotin‐dependent plant carboxylases (Alban et al ., 1993; Harwood, 1988; Wurtele and Nikolau, 1990) and one seed‐specific, biotinylated protein from pea (Duval et al ., 1994) have been identified.…”

Section: Introductionmentioning

confidence: 61%

“…Information on the mechanism of biotin uptake and allocation in plants has not been available. In baker's yeast and Escherichia coli , however, genes encoding biotin transporters have been cloned (Eisenberg, 1973; Stolz et al ., 1999). In both organisms the expression of these genes is regulated by the biotin concentration in the environment, and the respective gene products catalyse biotin‐H + symport across the plasma membranes (Eisenberg, 1974; Stolz et al ., 1999).…”

Section: Introductionmentioning

confidence: 99%

Plant sucrose‐H⁺ symporters mediate the transport of vitamin H

Ludwig

Stolz

Sauer³

2000

The Plant Journal

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Summary A cDNA coding for a vitamin H (biotin) transport protein from Arabidopsis was identified by genetic complementation of a biotin uptake‐deficient yeast mutant. Vitamin H transport by this protein was sensitive to the SH‐group inhibitor p‐chloromercuribenzene sulfonic acid (PCMBS) and to the uncoupler carbonyl cyanide‐m‐chlorophenylhydrazone (CCCP), suggesting an energy‐dependent biotin‐H+ symport mechanism. The transport activity could contribute to the so‐far uncharacterized plant sucrose‐H+ symporter AtSUC5 which mediates the energy‐dependent transport of biotin and sucrose, and restores growth of the biotin transport‐deficient yeast mutant on medium with low biotin concentrations. Functional comparison of the AtSUC5 transporter with previously characterized plant sucrose or monosaccharide transporters revealed that biotin transport may be a general and specific property of all plant sucrose transporters (sucrose/biotin‐H+ symporters). This first report on a transporter with dual substrate specificity for two structurally unrelated molecules has a major impact on general thinking concerning the specificity of membrane transporters. The physiological relevance of this finding is discussed.

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“…Biotin (vitamin H) is a small, sulfur-containing, cofactor which is covalently attached to a set of enzymes utilizing HCOs" in single-carbon transfer reactions , It was first described as a factor required for the growth of yeast, and was later isolated from dried egg yolks (Kogel and Tonnis, 1936) and from liver (Gyorgy and Langer Jr., 1968). It is an essential element in the diets of animals, and is biosynthesized by some plants and fungi, and the majority of microorganisms (Eisenberg, 1973;Eisenberg, 1987). Mutations in the biosynthesis or utilization of biotin are lethal in bacteria (Eisenberg, 1987), yeast (Mishina et ai, 1980), plants (Shellhanmier and Meinke, 1990), and animals (Wolf and Heard, 1989).…”

Section: Biotinmentioning

confidence: 99%

Biochemical and molecular biological characterization of plant acetyl-CoA carboxylases

Caffrey

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Biotin 3 Biotin Enzymes 5 Acetyl-CoA Carboxylase Plant Acetyl-CoA Carboxylase 17 Dissertation Organization CHAPTER 2: CHARACTERIZATION OF 60kDa BIOTIN-CONTAINING POLYPEPTIDE OF CARROT AS THE BIOTIN SUBUNIT OF AN ACETYL-CoA CARBOXYLASE Summary Introduction Materials and Methods Results Discussion 44 Literature Cited CHAPTER 3; TISSUE DISTRIBUTION OF ACETYL-CoA CARBOXYLASE IN LEAVES OF LEEK {Allium porrum L.) Summary Discussion 77 Acknowledgements 79 Literature Cited 84 CHAPTER 4: MOLECULAR CLONING OF A cDNA FOR, AND CHARACTERIZATION OF THE EXPRESSION OF, ACETYL-CoA CARBOXYLASE FROM SOYBEAN {Glycine max L.

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Biotin: Biogenesis, Transport, and Their Regulation

Cited by 29 publications

References 127 publications

Structure of a Putative Lipoate Protein Ligase from Thermoplasma acidophilum and the Mechanism of Target Selection for Post-translational Modification

Structure of a Putative Lipoate Protein Ligase from Thermoplasma acidophilum and the Mechanism of Target Selection for Post-translational Modification

Plant sucrose‐H⁺ symporters mediate the transport of vitamin H

Biochemical and molecular biological characterization of plant acetyl-CoA carboxylases

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Biotin: Biogenesis, Transport, and Their Regulation

Cited by 29 publications

References 127 publications

Structure of a Putative Lipoate Protein Ligase from Thermoplasma acidophilum and the Mechanism of Target Selection for Post-translational Modification

Structure of a Putative Lipoate Protein Ligase from Thermoplasma acidophilum and the Mechanism of Target Selection for Post-translational Modification

Plant sucrose‐H+ symporters mediate the transport of vitamin H

Biochemical and molecular biological characterization of plant acetyl-CoA carboxylases

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Plant sucrose‐H⁺ symporters mediate the transport of vitamin H