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. 1992 Jun;60(6):2317–2323. doi: 10.1128/iai.60.6.2317-2323.1992

Structure and function of a 40,000-molecular-weight protein antigen of Mycobacterium tuberculosis.

A B Andersen 1, P Andersen 1, L Ljungqvist 1
PMCID: PMC257160  PMID: 1587598

Abstract

A gene encoding a protein antigen from Mycobacterium tuberculosis with a molecular weight of 40,000 has been sequenced. On the basis of sequence homology and functional analyses, we demonstrated that the protein is an L-alanine dehydrogenase (EC 1.4.1.1). The enzyme was demonstrated in M. tuberculosis and Mycobacterium marinum but not in Mycobacterium bovis BCG. The enzyme may play a role in cell wall synthesis because L-alanine is an important constituent of the peptidoglycan layer. Although no consensus signal sequence was identified, we found evidence which suggests that the enzyme is secreted across the cell membrane. The enzyme was characterized and purified by chromatography, thus enabling further studies of its role in virulence and interaction with the immune system of M. tuberculosis-infected individuals.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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