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malS  -  periplasmic alpha-amylase

Escherichia coli UTI89

 
 
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Disease relevance of malS

  • The resulting plasmid was used as a probe to identify the intact malS gene in a lambda library of E. coli chromosomal HindIII fragments [1].
  • The malS-lacZ fusion was transferred onto a phage lambda vector and the 5' portion of malS was subcloned into pBR322 [1].
  • The alpha-amylase precursor from the bacterium Pseudoalteromonas haloplanktis possesses a propeptide at the C-terminus possibly responsible for outer membrane translocation [2].
 

High impact information on malS

  • In contrast, maeA, malS, and mleA had distinct roles in malate utilization for which they could compensate one another [3].
 

Associations of malS with chemical compounds

  • YtsJ activity, in contrast, was 70-fold higher with NADP+ than with NAD+, with Km values of 0.055 and 2.8 mM, respectively. lacZ fusions revealed strong transcription of ytsJ, twofold higher in malate than in glucose medium, but weak transcription of malS and mleA [3].

References

  1. Alpha-amylase of Escherichia coli, mapping and cloning of the structural gene, malS, and identification of its product as a periplasmic protein. Freundlieb, S., Boos, W. J. Biol. Chem. (1986) [Pubmed]
  2. The precursor of a psychrophilic alpha-amylase: structural characterization and insights into cold adaptation. Claverie, P., Vigano, C., Ruysschaert, J.M., Gerday, C., Feller, G. Biochim. Biophys. Acta (2003) [Pubmed]
  3. YtsJ has the major physiological role of the four paralogous malic enzyme isoforms in Bacillus subtilis. Lerondel, G., Doan, T., Zamboni, N., Sauer, U., Aymerich, S. J. Bacteriol. (2006) [Pubmed]
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