Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

bkdA2 - 2-oxoisovalerate dehydrogenase subunit beta

Pseudomonas putida KT2440

Hester, K. et al., Madhusudhan, K.T. et al., Burns, G. et al., Burns, G. et al.

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Disease relevance of bkdA2

Translation of bkdA1 and bkdA2 from an Escherichia coli expression plasmid produced only 45-kDa and 39-kDa proteins, with N-terminal methionine on the 39-kDa protein [1].

High impact information on bkdA2

Another construct containing the bkd promoter, bkdA1, and bkdA2 in pKT240 was used to transform P. putida JS113, a mutant which was unable to produce the E1 subunits of the branched-chain keto acid dehydrogenase [2].
The insertion of guanine residues 5' to the first ATG of bkdA2 did not affect expression of E1 beta in P. putida including the N-terminal leucine which appears to eliminate the possibility of ribosome jumping [1].
There was no intergenic space between bkdA2 and bkdB [3].

Biological context of bkdA2

Open reading frames encoding E1 alpha (bkdA1, 1233 bp) and E1 beta (bkdA2, 1020 bp) were identified with the aid of the N-terminal sequence of the purified subunits [4].

References

Purification of active E1 alpha 2 beta 2 of Pseudomonas putida branched-chain-oxoacid dehydrogenase. Hester, K., Luo, J., Burns, G., Braswell, E.H., Sokatch, J.R. Eur. J. Biochem. (1995) [Pubmed]
Transcriptional analysis of the promoter region of the Pseudomonas putida branched-chain keto acid dehydrogenase operon. Madhusudhan, K.T., Huang, G., Burns, G., Sokatch, J.R. J. Bacteriol. (1990) [Pubmed]
Comparison of the amino acid sequences of the transacylase components of branched chain oxoacid dehydrogenase of Pseudomonas putida, and the pyruvate and 2-oxoglutarate dehydrogenases of Escherichia coli. Burns, G., Brown, T., Hatter, K., Sokatch, J.R. Eur. J. Biochem. (1988) [Pubmed]
Similarity of the E1 subunits of branched-chain-oxoacid dehydrogenase from Pseudomonas putida to the corresponding subunits of mammalian branched-chain-oxoacid and pyruvate dehydrogenases. Burns, G., Brown, T., Hatter, K., Idriss, J.M., Sokatch, J.R. Eur. J. Biochem. (1988) [Pubmed]

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