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Insights to Sequence Information of Lactoylglutathione Lyase Enzyme from Different Source Organisms

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Author Affiliations

  • 1Department of Bioinformatics, UCST, Dehradun, INDIA
  • 2Department of Biotechnology, DDU University, Gorakhpur, INDIA
  • 3Department of Forest Pathology, FRI, Dehradun, INDIA

Int. Res. J. Biological Sci., Volume 1, Issue (6), Pages 38-42, October,10 (2012)

Abstract

Lactoylglutathione lyases (also known as glyoxalase I) are widely distributed enzymes among plants, fungi and bacteria. It is an enzyme that catalyzes the isomerization of hemithioacetal adducts, which are formed in a spontaneous reaction between a glutathionyl group and aldehydes such as methylglyoxal. In the present study, thirty full- length amino acid sequences of lactoylglutathione lyases from bacteria, fungi, and plants were collected and subjected to multiple sequence alignment (MSA), pattern identification, domain identification discovering individual amino acid composition, and phylogenetic tree construction. MSA revealed that one tyrosine residue were identically found in all analyzed species, two tyrosine, one arginine, one leucine, one glycine, one histidine, one phenylalanine, one proline, one aspartic acid and one glutamic acid residues were identically found in all the bacterial and fungal sources, one phenylalanine, one tyrosine, one histidine, one proline, and one glycine residues were identically found in all bacterial and plant sources while two glycine, two tyrosine, two aspartic acid and one proline residues were identically found in all plants and fungal lactoylglutathione lyases. Two major sequence clusters were constructed by phylogenetic analysis. One cluster contains ten species of fungi, five species of plant, and two species of bacteria, whereas the other one contains eight species of bacteria, four species of plant and one species of plant was outgrouped from both clusters. The amino acid composition result revealed that the average frequency of amino acid glycine is 7.86 percent that is very high in comparison to other amino acids and an average frequency of is 1.07 that is very low in all analyzed species. In addition, nine motifs which were unique for their groups were also identified.

References

  1. Ackerman R.S., Cozzarelli N.R. and Epstein W., Accumulation of toxic concentrations of methylglyoxal by wild-type Escherichia coli K-12, J. Bacteriol, 119, 357-362 (1974)
  2. Allen R.E., Lo T.W. and Thornalley P.J., Purification and characterisation of glyoxalase II from human red blood cells, Eur. J. Biochem., 213, 1261-1267 (1993)
  3. Banas J.A., Virulence properties of Streptococcus mutans, Front. Biosci., 9, 1267-1277 (2004)
  4. Cooper R.A., Metabolism of methylglyoxal in microorganisms, Annu. Rev. Microbiol., 38, 49-68 (1984)
  5. Eriksson S., Lucchini S., Thompson A., Rhen M., and Hinton J.C., Unravelling the biology of macrophage infection by gene expression profiling of intracellular Salmonella enterica, Mol. Microbiol, 47, 103-118 (2003)
  6. Freedberg W.B., Kistler W.S. and Lin E.C., Lethal synthesis of methylglyoxal by Escherichia coli during unregulated glycerol metabolism, J. Bacteriol, 108, 137-144 (1971)
  7. Frickel E.M., Jemth P., Widersten M. and Mannervik B., Yeast glyoxalase I is a monomeric enzyme with two active sites, J. Biol. Chem., 276, 1845-1849 (2001)
  8. Hanna M.N., Ferguson R.J., Li Y.H. and Cvitkovitch D.G., uvrA is an acid-inducible gene involved in the adaptive response to low pH in Streptococcus mutans, J. Bacteriol., 183, 5964-5973 (2001)
  9. Inoue Y. and Kimura A., Methylglyoxal and regulation of its metabolism in microorganisms, Adv. Microb. Physiol., 37, 177-227 (1995)
  10. Kalapos M.P., Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications, Toxicol. Lett., 110, 145-175 (1999)
  11. Khalichi P., Cvitkovitch D.G. and Santerre J.P., Effect of composite resin biodegradation products on oral streptococcal growth, Biomaterials,25, 5467-5472 (2004)
  12. Kim I., Kim E., Yoo S., Shin D., Min B., Song J. and Park C., Ribose utilization with an excess of mutarotase causes cell death due to accumulation of methylglyoxal, J. Bacteriol., 186, 7229-7235 (2004)
  13. Ko J., Kim I., Yoo S., Min B., Kim K. and Park C., Conversion of methylglyoxal to acetol by Escherichia colialdo-keto reductases, J. Bacteriol., 187, 5782-5789 (2005)
  14. Bailey T.L. and Elkan C., Expectation maximization pproach, Mach Learn, 21(1–2), 51–80 (1995)
  15. Dwivedi V.D. and Mishra S.K., Amino acid sequence analysis of glutamate dehydrogenase from different source organisms, Online J Bioinform., 13(2), 184-191 (2012)
  16. Bhatt T.K., Phylogenetic Studies on tRNA Dependent Amidotransferase from Plasmodium Falciparum,ISCA J. Biological Sci., 1(3), 20-24 (2012)