Thermostable ATP regeneration system using polyphosphate kinase from Thermosynechococcus elongatus BP-1 for d-amino acid dipeptide synthesis

Journal of Bioscience and Bioengineering

Volumn 103, Issue 2, 2007, Pages 179-184

  Sato, Masaru ^a   Masuda, Yusuke ^a   Kirimura, Kohtaro ^a   Kino, Kuniki ^a  

^a WASEDA UNIVERSITY   (Japan)

Author keywords

ATP regeneration; d alanine d alanine ligase; d amino acid dipeptide; polyphosphate kinase; thermophile

Indexed keywords

ATP REGENERATION; D-ALANINE-D-ALANINE LIGASE; D-AMINO ACID DIPEPTIDE; POLYPHOSPHATE KINASE; THERMOPHILE;

AMINO ACIDS; BIOCATALYSTS; BIOSYNTHESIS; HIGH TEMPERATURE EFFECTS; POLYPEPTIDES; THERMODYNAMIC STABILITY;

ENZYMES;

ADENOSINE; ADENOSINE TRIPHOSPHATE; DEXTRO ALANINE DEXTRO ALANINE LIGASE; DEXTRO AMINO ACID; DIPEPTIDE; ENZYME; POLYPHOSPHATE KINASE; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BIOCATALYST; CONTROLLED STUDY; COUPLING FACTOR; ENZYME SPECIFICITY; HIGH TEMPERATURE; MESOPHILE; NONHUMAN; PROTEIN SYNTHESIS; REGENERATION; THERMOPHILIC BACTERIUM; THERMOSTABILITY; THERMOSYNECHOCOCCUS ELONGATUS;

ADENOSINE TRIPHOSPHATE; BIOTECHNOLOGY; CYANOBACTERIA; DIPEPTIDES; ENZYME STABILITY; HEAT; PHOSPHOTRANSFERASES (PHOSPHATE GROUP ACCEPTOR);

THERMOSYNECHOCOCCUS ELONGATUS BP-1; THERMOTOGA MARITIMA;

EID: 33947166251     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.103.179     Document Type: Article

References (24)

1. Shin Y., and Whitesides G.M. Large-scale ATP-requireing enzymatic phosphorylation of creatine can be driven by enzymatic ATP regeneration. J. Org. Chem. 42 (1977) 4165-4166
2. Widjaja A., Ogino H., Yasuda M., Ishimi K., and Ishikawa H. Experimental investigation of fructose 1,6-diphosphate production and simultaneous ATP regeneration by conjugated enzymes in an ultrafiltration hollow-fiber reactor. J. Biosci. Bioeng. 88 (1999) 640-645
3. Lee H.C., Lee S., Sohng J.K., and Liou K. One-pot enzymatic synthesis of UDP-d-glucose from UMP and glucose-1-phosphate using and ATP regeneration system. J. Biochem. Mol. Biol. 37 (2004) 503-506
4. Widjaja A., Shiroshima M., Yasuda M., Ogino H., Nakajima H., and Ishikawa H. Enzymatic synthesis of fructose 1,6-diphosphate with ATP regeneration in a batch reactor and a semibatch reactor using purified enzymes of Bacillus stearothermophilus. J. Biosci. Bioeng. 87 (1999) 611-618
5. Shiroshima M., Widjaja A., Yasuda M., Ogino H., Ishimi K., and Ishikawa H. Theoretical investigation of fructose 1,6-diphosphate production and simultaneous ATP regeneration by conjugated enzymes in an ultrafiltration hollow-fiber reactor. J. Biosci. Bioeng. 88 (1999) 632-639
6. Shiba T., Tsutsumi K., Ishige K., and Noguchi T. Inorganic polyphosphate and polyphosphate kinase: their novel bioogical functions and applications. Biochemistry (Moscow) 65 (2000) 315-323
7. Resnick S.M., and Zehnder A.J.B. In vitro ATP regeneration from polyphosphate and AMP by polyphosphate: AMP phosphotransferase and adenylate kinase from Acinetobacter johnsonii 210A. Appl. Environ. Microbiol. 66 (2000) 2045-2051
8. Kameda A., Shiba T., Kawazoe Y., Satoh Y., Ihara Y., Munekata M., Ishige K., and Noguchi T. A novel ATP regeneration system using polyphosphate-AMP phosphotransferase and polyphosphate kinase. J. Biosci. Bioeng. 91 (2001) 557-563
9. Li Y., Wei G., and Chen J. Glutathione: a review on biotechnological production. Appl. Microbiol. Biotechnol. 66 (2004) 233-242
10. Yamamoto S., Uchimura K., Wakayama M., and Tachiki T. Purification and characterization of glutamine synthetase of Pseudomonas taetrolens Y-30: an enzyme usable for production of theanine by coupling with the alcoholic fermentation system of baker's yeast. Biosci. Biotechnol. Biochem. 68 (2004) 1888-1897
11. Tabata K., Ikeda H., and Hashimoto S. ywfE in Bacillus subtilis codes for a novel enzyme, l-amino acid ligase. J. Bacteriol. 187 (2005) 5195-5202
12. Sato M., Kirimura K., and Kino K. d-Amino acid dipeptide production utilizing d-alanine-d-alanine ligases with novel substrate specificity. J. Biosci. Bioeng. 99 (2005) 623-628
13. Kim D., and Swartz J.R. Regeneration of adenosine triphosphate from glycolytic intermediates for cell-free protein synthesis. Biotechnol. Bioeng. 74 (2001) 309-316
14. Wakisaka S., Ohshima Y., Ogawa M., Tochikura T., and Tachiki T. Characteristics and efficiency of glutamine production by coupling of a bacterial glutamine synthetase reaction with the alcoholic fermentation system of baker's yeast. Appl. Environ. Microbiol. 64 (1998) 2952-2957
15. Yamamoto S., Wakayama M., and Tachiki T. Theanine production by coupled fermentation with energy transfer employing Pseudomonas taetrolens Y-30 glutamine synthetase and baker's yeast cells. Biosci. Biotechnol. Biochem. 69 (2005) 784-789
16. Yagasaki M., Tabata K., Ikeda H., and Hashimoto S. Development of efficient dipeptide manufacturing. Bioindustry 23 (2006) 26-34
17. Mignogna G., Simmaco M., Greil G., and Barra D. Antibacterial and haemolytic peptides containing d-alloisoleucine from the skin of Bombina variegata. EMBO J. 12 (1993) 4829-4832
18. Barra D., and Simmaco M. Amphibian skin: a promising resource for antimicrobial peptides. Trends Biotechnol. 13 (1995) 205-209
19. Kreil G. d-Amino acids in animal peptides. Annu. Rev. Biochem. 66 (1997) 337-345
20. Avrahami D., Oren Z., and Shai Y. Effect of multiple aliphatic amino acids substitutions on the suructure, function, and mode of action of diastereomeric membrane active peptides. Biochemistry 40 (2001) 12591-12603
21. Papo N., Oren Z., Pag U., Sahl H.G., and Shai Y. The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers. J. Biol. Chem. 277 (2002) 33913-33921
22. Sato M., Kirimura K., and Kino K. Substrate specificity of thermostable d-alanine-d-alanine ligase from Thermotoga maritima ATCC 43589. Biosci. Biotechnol. Biochem. 70 (2006) 2790-2792
23. Kornberg A., Kornberg S.R., and Simms E.S. Metaphosphate synthesis by an enzyme from Escherichia coli. Biochem. Biophys. Acta 20 (1956) 215-227
24. Kuroda A., and Kornberg A. Polyphosphate kinase as a nucleoside diphosphate kinase in Escherichia coli and Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. USA 99 (1997) 439-442