The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

malP  -  maltodextrin phosphorylase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3404, JW5689, blu, malA
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of malP


High impact information on malP


Chemical compound and disease context of malP


Biological context of malP


Associations of malP with chemical compounds

  • Uninduced malPQ transcription, as followed by measuring beta-galactosidase expression in a strain carrying a malP-lacZ hybrid gene and grown in the absence of maltose, requires the presence of CAP [18].
  • The bacterial enzyme maltodextrin phosphorylase (MalP) catalyses the phosphorolysis of an alpha-1,4-glycosidic bond in maltodextrins, removing the non-reducing glucosyl residues of linear oligosaccharides as glucose-1-phosphate (Glc1P) [19].
  • The MalT sites in malPp were precisely located and their occupation as a function of MalT concentration was quantified using DNase I and dimethyl sulphate footprinting experiments [20].
  • Likewise, in an in vitro transcription system, initiation of transcription at malPp required the presence of the MalT protein and maltotriose along with the RNA polymerase holoenzyme; neither maltose nor maltotetraose could substitute for maltotriose [21].

Regulatory relationships of malP

  • Using in vitro techniques we have fused upstream sequences from the malPp promoter (normally activated by the MalT protein) to downstream sequences from the lacZp promoter (normally repressed by the LacI protein) [22].

Other interactions of malP

  • The sequences of the coding regions and of elements known to be important for the functions of these two promoters in E. coli were well conserved between the two bacteria, whereas the sequence of the malT-malP intergenic region had totally diverged [23].
  • The cloned region which follows glgA contains an incomplete ORF (1149 bp), glgY, which appears to encode 383 aa of the N terminus of glycogen phosphorylase, based upon sequence similarity with the enzyme from rabbit muscle (47% identical aa residues) and with maltodextrin phosphorylase from E. coli (37% identical aa residues) [24].

Analytical, diagnostic and therapeutic context of malP


  1. Escherichia coli K-12 tolF mutants: alterations in protein composition of the outer membrane. Chai, T.J., Foulds, J. J. Bacteriol. (1977) [Pubmed]
  2. Restriction map of the Escherichia coli malA region and identification of the malT product. Raibaud, O., Schwartz, M. J. Bacteriol. (1980) [Pubmed]
  3. Genetic localization and regulation of the maltose phosphorylase gene, malP, in Lactococcus lactis. Nilsson, U., Rådström, P. Microbiology (Reading, Engl.) (2001) [Pubmed]
  4. Structural relationships among regulated and unregulated phosphorylases. Buchbinder, J.L., Rath, V.L., Fletterick, R.J. Annual review of biophysics and biomolecular structure. (2001) [Pubmed]
  5. The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase. Watson, K.A., Schinzel, R., Palm, D., Johnson, L.N. EMBO J. (1997) [Pubmed]
  6. Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase. O'Reilly, M., Watson, K.A., Schinzel, R., Palm, D., Johnson, L.N. Nat. Struct. Biol. (1997) [Pubmed]
  7. Active site lysine promotes catalytic function of pyridoxal 5'-phosphate in alpha-glucan phosphorylases. Schinzel, R. J. Biol. Chem. (1991) [Pubmed]
  8. Purification and properties of the MalT protein, the transcription activator of the Escherichia coli maltose regulon. Richet, E., Raibaud, O. J. Biol. Chem. (1987) [Pubmed]
  9. The crystal structure of the Escherichia coli maltodextrin phosphorylase-acarbose complex. O'Reilly, M., Watson, K.A., Johnson, L.N. Biochemistry (1999) [Pubmed]
  10. Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli. Griessler, R., D'auria, S., Schinzel, R., Tanfani, F., Nidetzky, B. Biochem. J. (2000) [Pubmed]
  11. Pyridoxal 5'-phosphate as a 31P reporter observing functional changes in the active site of Escherichia coli maltodextrin phosphorylase after site-directed mutagenesis. Schinzel, R., Palm, D., Schnackerz, K.D. Biochemistry (1992) [Pubmed]
  12. Activation of E350A mutant maltodextrin phosphorylase by exogenously added acetate. Drueckes, P., Schinzel, R. Protein Eng. (1996) [Pubmed]
  13. Maltodextrin phosphorylase from Escherichia coli: production and application for the synthesis of alpha-glucose-1-phosphate. Nidetzky, B., Weinhäusel, A., Haltrich, D., Kulbe, K.D., Schinzel, R. Ann. N. Y. Acad. Sci. (1996) [Pubmed]
  14. Use of deletions created in vitro to map transcriptional regulatory signals in the malA region of Escherichia coli. Raibaud, O., Débarbouillé, M., Schwartz, M. J. Mol. Biol. (1983) [Pubmed]
  15. E. coli maltodextrin phosphorylase: primary structure and deletion mapping of the C-terminal site. Palm, D., Goerl, R., Weidinger, G., Zeier, R., Fischer, B., Schinzel, R. Z. Naturforsch., C, J. Biosci. (1987) [Pubmed]
  16. Essential and nonessential sequences in malPp, a positively controlled promoter in Escherichia coli. Raibaud, O., Gutierrez, C., Schwartz, M. J. Bacteriol. (1985) [Pubmed]
  17. A technique for integrating any DNA fragment into the chromosome of Escherichia coli. Raibaud, O., Mock, M., Schwartz, M. Gene (1984) [Pubmed]
  18. Indirect effects of the 3'-5' cyclic adenosine monophosphate binding protein (CAP) on the transcription of the malPQ operon in Escherichia coli. Gutierrez, C., Chapon, C., Schwartz, M. Biochimie (1985) [Pubmed]
  19. Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase. Geremia, S., Campagnolo, M., Schinzel, R., Johnson, L.N. J. Mol. Biol. (2002) [Pubmed]
  20. Multiple protein-DNA and protein-protein interactions are involved in transcriptional activation by MalT. Danot, O., Raibaud, O. Mol. Microbiol. (1994) [Pubmed]
  21. Maltotriose is the inducer of the maltose regulon of Escherichia coli. Raibaud, O., Richet, E. J. Bacteriol. (1987) [Pubmed]
  22. The mac promoters: functional hybrid promoters activated by the malT product and repressed by the lacI product. Vidal-Ingigliardi, D., Raibaud, O. Nucleic Acids Res. (1985) [Pubmed]
  23. Comparison of the malA regions of Escherichia coli and Klebsiella pneumoniae. Bloch, M.A., Raibaud, O. J. Bacteriol. (1986) [Pubmed]
  24. Analysis of the Escherichia coli glycogen gene cluster suggests that catabolic enzymes are encoded among the biosynthetic genes. Romeo, T., Kumar, A., Preiss, J. Gene (1988) [Pubmed]
  25. Dissecting differential binding in the forward and reverse reaction of Escherichia coli maltodextrin phosphorylase using 2-deoxyglucosyl substrates. Becker, S., Palm, D., Schinzel, R. J. Biol. Chem. (1994) [Pubmed]
  26. Crystallization and crystallographic data of Escherichia coli maltodextrin phosphorylase. Buehner, M. FEBS Lett. (1978) [Pubmed]
  27. Efficient downstream processing of maltodextrin phosphorylase from Escherichia coli and stabilization of the enzyme by immobilization onto hydroxyapatite. Eis, C., Griessler, R., Maier, M., Weinhäusel, A., Bock, B., Kulbe, K.D., Haltrich, D., Schinzel, R., Nidetzky, B. J. Biotechnol. (1997) [Pubmed]
WikiGenes - Universities