A cluster of Thermotoga neapolitana genes involved in the degradation of starch and maltodextrins: The molecular structure of the locus

Molekulyarnaya Biologiya

Volumn 37, Issue 5, 2003, Pages 801-809

  Berezina, O V ^a   Lunina, N A ^a   Zverlov, V V ^a   Naumoff, D G ^b   Liebl, W ^c   Velikodvorskaya, G A ^a  

^a INSTITUTE OF MOLECULAR GENETICS   (Russian Federation)

^b STATE RESEARCH INSTITUTE OF GENETICS AND SELECTION OF INDUSTRIAL MICROORGANISMS   (Russian Federation)

^c UNIVERSITY OF GÖTTINGEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GLUCOSIDASE; BACTERIAL PROTEIN; DEAMINASE; DNA FRAGMENT; GLUCOSE; MALTODEXTRIN; PROTEIN AG1A; PROTEIN AG1B; PROTEIN MALG; RIBOFLAVIN; STARCH; UNCLASSIFIED DRUG; DNA; POLYSACCHARIDE; RNA; RNA PRIMERS;

AMINO ACID SEQUENCE; ARTICLE; BASE PAIRING; CHEMICAL STRUCTURE; CONTROLLED STUDY; DEGRADATION; ESCHERICHIA COLI; GENE; GENE CLUSTER; GENE LOCUS; GENE SEQUENCE; HYDROLYSIS; MOLECULAR CLONING; NONHUMAN; PHYLOGENY; PROTEIN FAMILY; RIBD GENE; SEQUENCE HOMOLOGY; THERMOTOGA MARITIMA; THERMOTOGA NEAPOLITANA; ENZYME SPECIFICITY; GENETICS; GRAM NEGATIVE ANAEROBIC BACTERIA; METABOLISM; MOLECULAR GENETICS; MULTIGENE FAMILY; NUCLEOTIDE SEQUENCE; PLASMID;

BACTERIA (MICROORGANISMS); THERMOTOGA MARITIMA; THERMOTOGA NEAPOLITANA;

AMINO ACID SEQUENCE; BASE SEQUENCE; DNA; GRAM-NEGATIVE ANAEROBIC STRAIGHT, CURVED, AND HELICAL RODS; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; PLASMIDS; POLYSACCHARIDES; RNA; STARCH; SUBSTRATE SPECIFICITY;

EID: 1542496458     PISSN: 00268984     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (17)

1. Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S., Phillips CA., Richardson D., Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. 1999. Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature. 399, 323-329.
2. Huber R., Steuer K.O. The Order Thermotogales. In: The Procaryotes. A Handbook on the Biology of Bacteria, Ecophysiology, Isolation, Identification, Applications. N.Y.: Springer-Verlag, 1992. V. II. P. 3809-3815.
3. Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Sedman J.G., Smith J.A., Struhl K. 1987. Current protocols in molecular biology. N.Y.: John Wiley and Sons.
4. Sambrook J., Fritsch E.F., Maniatis E. 1989. Molecular cloning: A Laboratory Manual. 2nd ed. Cold Spring Harbor, N. Y.: Cold Spring Harbor Laboratory Press.
5. Dassa E. 1993. Sequence - function relationships in MalG, an inner membrane protein from the maltose transport system in Escherichia coli. Mol. Microbiol. 7, 39-47.
6. Lee M.H., Kim Y.W., Kim T.J., Park C.S., Kim J.W., Moon T.W., Park K.H. 2002. A novel amylolytic enzyme from Thermotoga maritima, resembling cyclodextrinase and α-glucosidase, that liberates glucose from the reducing end of the substrates. Biochem. Biophys. Res. Commun. 295, 818-825.
7. Bibel M., Brettl C., Gosslar U., Kriegshäuser G., Liebl W. 1998. Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium T. maritima. FEMS Microbiol. Lett. 158, 9-15.
8. 2+-, and thiol-dependent α-glucosidase. Extremophiles. 4, 189-200.
9. Liebl W., Stemplinger I., Ruile P. 1997. Properties and gene structure of the Thermotoga maritima α-amylase AmyA, a putative lipoprotein of a hyperthermophilic bacterium. J. Bacteriol. 179, 941-948.
10. Henrissat B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280, 309-316.
11. Kuriki T., Imanaka T. 1999. The concept of the α-amylase family: structural similarity and common catalytic mechanism. J. Biosci. Bioeng. 87, 557-565.
12. Park K.-H., Kim T.-J., Cheong T.-K., Kim J.-W., Oh B.-H., Svensson B. 2000. Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family. Biochim. Biophys. Acta. 1478, 165-185.
13. Thompson J., Pikis A., Ruvinov S.B., Henrissat B., Yamamoto H., Sekiguchi J. 1998. The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-alpha-glucosidase. Assignment to family 4 of the glycosylhydrolase superfamily. J. Biol. Chem. 273, 27347-27356.
14. + binding by the Thermotoga maritima alpha-glucosidase AglA, a member of glycoside hydrolase family 4. FEBS Lett. 517, 267-271.
15. Thompson J., Ruvinov S.B., Freedberg D.I., Hall B.G. 1999. Cellobiose-6-phosphate hydrolase (CelF) of Escherichia coli: characterization and assignment to the unusual family 4 of glycosylhydrolases. J. Bacteriol. 181, 7339-7345.