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Gene Review:

cma1 - cyclopropane-fatty-acyl-phospholipid synthase

Mycobacterium tuberculosis CDC1551

Yuan, Y. et al., Yuan, Y. et al., George, K.M. et al.

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Disease relevance of cma1

This activity was localized to a single gene (cma1) encoding a protein that was 34% identical to the cyclopropane fatty acid synthase from Escherichia coli [1].

High impact information on cma1

Using the gene for the enzyme that introduces the distal cyclopropane (cma1) as a probe, we have cloned and sequenced a cluster of genes coding for four highly homologous methyl transferases (mma1-4) [2].
M. smegmatis overexpressing the cma1 gene product significantly resist killing by hydrogen peroxide, suggesting that this modification may be an important adaptation of slow-growing mycobacteria to oxidative stress [1].
This gene, named cma2, was sequenced and found to be 52% identical to cma1 (which cyclopropanates the distal double bond) and 73% identical to the gene from M. leprae [3].

References

Identification of a gene involved in the biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Yuan, Y., Lee, R.E., Besra, G.S., Belisle, J.T., Barry, C.E. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic acids in Mycobacterium tuberculosis. Yuan, Y., Barry, C.E. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
The biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Identification and functional analysis of CMAS-2. George, K.M., Yuan, Y., Sherman, D.R., Barry, C.E. J. Biol. Chem. (1995) [Pubmed]

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