Biochemical and genetic characterization of a novel enzyme of pentitol metabolism: D-arabitol-phosphate dehydrogenase

Biochemical Journal

Volumn 371, Issue 1, 2003, Pages 191-197

  Povelainen, Mira ^a   Eneyskaya, Elena V ^b   Kulminskaya, Anna A ^b   Ivanen, Dina R ^b   Kalkkinen, Nisse ^c   Neustroev, Kirill N ^b   Miasnikov, Andrei N ^a  

^a Danisco Finland Oy   (Finland)

^b PETERSBURG NUCLEAR PHYSICS INSTITUTE   (Russian Federation)

^c UNIVERSITY OF HELSINKI   (Finland)

Author keywords

Enterococcus avium; NADH dependent dehydrogenase; Pentitol phosphate metabolism; Xylulose 5 phosphate

Indexed keywords

DNA; ENZYMES; GENETIC ENGINEERING; PROTEINS;

MOLECULAR MASS;

BIOCHEMISTRY;

ARABINITOL; DEXTRO ARABITOL PHOSPHATE DEHYDROGENASE; MANGANESE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PHOSPHOTRANSFERASE; RIBITOL; UNCLASSIFIED DRUG; XYLITOL; XYLULOSE; ZINC; ALDEHYDE REDUCTASE; ARABITOL 5 PHOSPHATE; ARABITOL-5-PHOSPHATE; BACTERIAL PROTEIN; METAL; PENTOSE PHOSPHATE; RECOMBINANT PROTEIN; SUGAR PHOSPHATE; XYLULOSE 5 PHOSPHATE; XYLULOSE-5-PHOSPHATE;

AMINO ACID SEQUENCE; ARTICLE; BIOCHEMISTRY; CATABOLISM; CELL LYSATE; DNA SEQUENCE; ENTEROCOCCUS AVIUM; ENZYME METABOLISM; ENZYME PURIFICATION; ENZYME SPECIFICITY; GENETICS; GRAM POSITIVE BACTERIUM; MOLECULAR WEIGHT; NONHUMAN; OPERON; OXIDATION; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; CHEMISTRY; ENTEROCOCCUS; ENZYMOLOGY; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; SEQUENCE ANALYSIS;

BACTERIA (MICROORGANISMS); ENTEROCOCCUS AVIUM; POSIBACTERIA; PROKARYOTA;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; BIOCHEMISTRY; ENTEROCOCCUS; KINETICS; METALS; MOLECULAR SEQUENCE DATA; NAD; NADP; OXIDATION-REDUCTION; PENTOSEPHOSPHATES; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS; SUBSTRATE SPECIFICITY; SUGAR ALCOHOL DEHYDROGENASES; SUGAR PHOSPHATES;

EID: 0242286156     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021096     Document Type: Article

References (30)

1. Wehmeier, U. F. and Lengeler, J. W. (1994) Sequence of the sor-operon for I-sorbose utilization from Klebsrella pneumoniae KAY2026. Biochim. Biophys. Acta 1208, 348-351
2. Novotny, M. J., Reizer, J., Esch, F. and Saier, Jr, M. H. (1984) Purification and properties of D-mannitol-1-phosphate dehydrogenase and D-glucitol-6-phosphate dehydrogenase from Escherichia coli. J. Bacteriol. 159, 986-990
3. Honeyman, A. L. and Curtiss, 3rd, R. (1992) Isolation, characterization, and nucleotide sequence of the Streptococcus mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific factor III gene of the phosphoenolpyruvate phosphotransferase system. Infect. Immun. 60, 3369-3375
4. Nobelmann, B. and Lengeler, J. W. (1995) Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262, 69-72
5. London, J. and Chace, N. M. (1977) New pathways for the metabolism of pentitols. Proc. Natl. Acad. Sci. U.S.A. 74, 4296-4300
6. Hausman, S. Z. and London, J. (1987) Purification and characterization of ribitol-5-phosphate and xylitol-5-phosphate dehydrogenases from strains of Lactobacillus casei. J. Bacteriol. 169, 1651-1655
7. Waler, S. M., Rolla, G., Assev, S. and Ciardi, J. E. (1984) The effect of xylitol on plaque metabolism. Swed. Dent. J. 8, 155-161
8. Scangos, G. A. and Reiner, A. M. (1978) Ribitol and D-arabitol catabolism in Escherichia coli. J. Bacteriol. 134, 492-500
9. Neuberger, M. S., Patterson, A. R. A. and Hartley, B. S. (1979) Purification and properties of Klebsiella aerogenes arabitol dehydrogenase. Biochem. J. 183, 31-42
10. Wong, B., Leeson, S., Grindle, S., Magee, B., Brooks, E. and Magee, P. T. (1995) D-Arabitol metabolism in Candida albicans: construction and analysis of mutants lacking D-arabitol dehydrogenase. J. Bacteriol. 177, 2971-2976
11. Barnwell, J. L., Saunders, W. A. and Watson, R. W. (1955) Synthesis and characterization of D-xylofuranose-5-phosphate. Can. J. Chem. 33, 711-715
12. Savel'ev, A. N., Eneyskaya, E. V., Isaeva-Ivanova, L. S., Shabalin, K. A., Golubev, A. M. and Neustroev, K. N. (1997) The carbohydrate moiety of α-galactosidase from Trichoderma reesei. Glycoconj. J. 14, 897-905
13. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
14. Lowry, O. H., Rosenbrough, N. J., Farr, A. L. and Randall, R. J. (1951) Protein measurements with the Folin phenol reagent. J. Biol. Chem. 193, 265-275
15. Sambrook, J., Fritsch, E. F. and Maniatis, T. (1989) Molecular Cloning: a Laboratory Manual, 2nd edn, Cold Spring Harbor Press, Cold Spring Harbor, NY
16. Omburo, G. A., Kuo, J. M., Mullins, L. S. and Raushel, F. M. (1992) Characterization of the zinc binding site of bacterial phosphotriesterase. J. Biol. Chem. 267, 13278-13283
17. 2+ bound to a soluble β-galactoside binding hepatic lectin. FEBS Lett. 360, 285-288
18. Heppel, S., Harkness, D. and Hilmoe, R. (1962) A study of the substrate specificity and other properties of the alkaline phosphatase of Escherichia coli. J. Biol. Chem. 237, 841-845
19. Jörnvall, H., Danielson, O., Ecklund, H., Helmqvist, L., Höög, J.-O., Pares, X. and Shafcat, J. (1993) Enzyme and isoenzyme developments within the medium-chain alcohol dehydrogenase family. In Enzymology and Molecular Biology of Carbonyl Metabolism, vol. 4 (Weiner, H., Crabb, D. and Flynn, T. G., eds.), pp. 533-544, Plenum, New York
20. Nyman, T. A., Matikainen, S., Sareneva, T., Julkunen, I. and Kalkkinen, N. (2000) Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon-α-regulated genes. Eur. J. Biochem. 267, 4011-4019
21. Dorokhov, Y. L., Mäkinen, K., Frolova, O. Y., Merits, A., Saarinen, J., Kalkkinen, N., Atabekov, J. G. and Saarma, M. (1999) A novel function for a ubiquitous plant enzyme pectin methylesterase: the host-cell receptor for the tobacco mosaic virus movement protein. FEBS Lett. 461, 223-228
22. Cutting, S. M. and Vander Horn, P. B. (1990) Genetic analysis. In Molecular Biological Methods for Bacillus (Harwood, C. R. and Cutting, S. M., eds.), pp 27-74, John Wiley and Sons, Chichester
23. Kerovuo, J., von Weymarn, N., Povelainen, M., Auer, S. and Miasnikov, A. (2000) A new efficient expression system for Bacillus and its application to production of recombinant phytase. Biotechnol. Lett. 22, 1311-1317
24. Yang, M., Ferrari, E., Chen, E. and Henner, D. J. (1986) Identification of the pleiotropic sacQ gene of Bacillus subtilis. J Bacteriol. 166, 113-119
25. Hueck, C. J., Hillen, W. and Saier, M. H. (1994) Analysis of a sequence mediating catabolite repression in Gram-positive bacteria. Res. Microbiol. 145, 503-518
26. Bron, S. (1990) Plasmids. In Molecular Biological Methods for Bacillus (Harwood, C. R. and Cutting, S. M., eds), pp. 148-149, John Wiley and Sons, Chichester
27. 2+ activation of and binding to yeast enolase: functional study. Biochemistry 31, 2165-2171
28. Marini, I., Bucchioni, L., Borella, P., Del Corso, A. and Mura, U. (1997) Sorbitol dehydrogenase from bovine lens: purification and properties. Arch. Biochem. Biophys. 340, 383-391
29. Epperly, B. R. and Dekker, E. E. (1991) L-Threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. J. Biol. Chem. 266, 6086-6092
30. Saklani-Justoforges, H., Fontan, E. and Goosens, P. L. (2001) Characterisation of a Listeria monocytogenes mutant deficient in D-arabitol fermentation. Res. Microbiol. 152, 175-177