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Gene Review:

lplA - lipoate-protein ligase A

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4378, JW4349, slr, yjjF

Kim, d.o. .J. et al., Morris, T.W. et al., Fujiwara, K. et al., Morris, T.W. et al., Gómez, A. et al.

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Disease relevance of lplA

Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein [1].
A gene called lplA (lipoprotein-like) has been isolated from a genomic library of Bacillus subtilis expressed in Escherichia coli [2].

High impact information on lplA

First, LplA activates exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP [3].
Lipoyl-AMP is bound deeply in the bifurcated pocket of LplA and adopts a U-shaped conformation [3].
This first view of the activated intermediate bound to LplA allowed us to propose a model of the complexes between Ta LplA and lipoyl domains, thus shedding light on the target protein/lysine residue specificity of LplA [3].
The overall fold of LplA bears some resemblance to that of the biotinyl protein ligase module of the E. coli biotin holoenzyme synthetase/bio repressor (BirA) [3].
The predicted amino acid sequence showed 35% identity with that of Escherichia coli lipoate-protein ligase A. Northern and Southern blot analyses showed a single band, and a single species of mRNA for lipoyltransferase was found by reverse transcription-polymerase chain reaction [4].

Biological context of lplA

The lplA gene has been cloned, sequenced, and physically mapped to min 99.6 (4657 kilobases) of the E. coli chromosome [5].
Clones carrying the lplA gene were selected by the ability of the colonies to give visible haloes of starch hydrolysis [2].

Associations of lplA with chemical compounds

Recently we described the isolation of the lplA locus, the first gene known to encode a lipoyl-protein ligase for the attachment of lipoyl groups to lipoate-dependent apoenzymes (T. W. Morris, K. E. Reed, and J. E. Cronan, Jr., J. Biol. Chem. 269:16091-16100, 1994) [1].

Other interactions of lplA

Here, we report an unexpected redundancy between the functions of lplA and lipB, a gene previously identified as a putative lipoate biosynthetic locus [1].

Analytical, diagnostic and therapeutic context of lplA

Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product [5].

References

Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein. Morris, T.W., Reed, K.E., Cronan, J.E. J. Bacteriol. (1995) [Pubmed]
The Bacillus subtilis lipoprotein LplA causes cell lysis when expressed in Escherichia coli. Gómez, A., Ramón, D., Sanz, P. Microbiology (Reading, Engl.) (1994) [Pubmed]
Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains. Kim, d.o. .J., Kim, K.H., Lee, H.H., Lee, S.J., Ha, J.Y., Yoon, H.J., Suh, S.W. J. Biol. Chem. (2005) [Pubmed]
Cloning and expression of a cDNA encoding bovine lipoyltransferase. Fujiwara, K., Okamura-Ikeda, K., Motokawa, Y. J. Biol. Chem. (1997) [Pubmed]
Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product. Morris, T.W., Reed, K.E., Cronan, J.E. J. Biol. Chem. (1994) [Pubmed]

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