Taxonomy of the Streptomyces strain ZG0656 that produces acarviostatin α-amylase inhibitors and analysis of their effects on blood glucose levels in mammalian systems

Journal of Applied Microbiology

Volumn 106, Issue 2, 2009, Pages 525-533

  Geng, P ^a,b   Bai, G ^a   Shi, Q ^a   Zhang, L ^a   Gao, Z ^a   Zhang, Q ^a  

^a NANKAI UNIVERSITY   (China)

^b TIANJIN MEDICAL UNIVERSITY   (China)

Author keywords

Acarviosine; Acarviostatin; Polyphasic taxonomy; Streptomyces coelicoflavus var. nankaiensis; amylase inhibitor

Indexed keywords

BACTERIA; BLOOD; GLUCOSE; MAMMALS; OLIGOMERS; TAXONOMIES; VALUE ENGINEERING;

ACARVIOSINE; ACARVIOSTATIN; BLOOD GLUCOSE LEVEL; MAMMALIAN SYSTEMS; NANKAIENSIS; POLYPHASIC; POLYPHASIC TAXONOMY; STREPTOMYCES COELICOFLAVU VAR.; TAXONOMIC STATUS; Α-AMYLASE INHIBITOR;

AMYLASES;

ACARVIOSTATIN I03; ACARVIOSTATIN II03; ACARVIOSTATIN III03; ACARVIOSTATIN IV03; AMYLASE; AMYLASE INHIBITOR; GLUCOSE; OLIGOMER; STARCH; UNCLASSIFIED DRUG;

BACTERIUM; BIOACTIVITY; DIABETES; DISEASE CONTROL; ENZYME ACTIVITY; GLUCOSE; HYDROLYSIS; MAMMAL; MICROBIAL ACTIVITY; SECONDARY METABOLITE; TAXONOMY;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BACTERIAL STRAIN; BLOOD SAMPLING; CONTROLLED STUDY; GLUCOSE BLOOD LEVEL; GLUCOSE TRANSPORT; HYDROLYSIS; IN VITRO STUDY; IN VIVO STUDY; MAMMAL; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; STREPTOMYCES; STREPTOMYCES COELICOFLAVUS; TAXONOMY;

MAMMALIA; STREPTOMYCES; STREPTOMYCES COELICOFLAVUS; SUS;

EID: 58549096546     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/j.1365-2672.2008.04021.x     Document Type: Article

References (21)

1. Altschul, S.F., Madden, T.L., Schäffer, A.A., Zhang, J., Zhang, Z., Miller, W. Lipman, D.J. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25, 3389 3402.
2. Becker, B., Lechevalier, M.P. Lechevalier, H.A. (1965) Chemical composition of cell-wall preparation from strains of various form - genera aerobic actinomycetes. Appl Microbiol 13, 236 243.
3. Cui, X.L., Mao, P.H., Zeng, M., Li, W.J., Zhang, L.P., Xu, L.H. Jiang, C.L. (2001) Streptimonospora salina gen. nov., sp. nov., a new member of the family Nocardiopsaceae. Int J Syst Evol Microbiol 51, 357 363.
4. Geng, P., Yang, Y., Gao, Z., Yu, Y., Shi, Q. Bai, G. (2007) Combined effect of total alkaloids from Feculae bombycis and natural flavonoids on diabetes. J Pharm Pharmacol 59, 1145 1150.
5. Geng, P., Qiu, F., Zhu, Y. Bai, G. (2008) Four acarviosin-containing oligosaccharides identified from Streptomyces coelicoflavus ZG0656 are potent inhibitors of α-amylase. Carbohydr Res 343, 882 892.
6. Hiele, M., Ghoos, Y., Rutgeerts, P. Vantrappen, G. (1992) Effects of acarbose on starch hydrolysis. Study in healthy subjects, ileostomy patients, and in vitro. Dig Dis Sci 37, 1057 1064.
7. Jiang, L.Y., Li, M.G., Li, W.J., Cui, X.L., Xu, L.H. Jiang, C.L. (2001) Study on the application of quantitative analysis of cell-wall amino acids in actinomycetes. Acta Microbiol Sin 41, 270 277.
8. Lechevalier, H.A. (1989) Genus Streptomyces Waksman and Henrici, 1943. In Bergey's Manual of Systematic Bacteriology: Genas Streptomyces, vol. 4. ed. Williams, S.T., Sharpe, M.E. Holt, J.G. pp. 2344 2347. Baltimore, MD : Williams & Wilkins.
9. Li, C., Begum, A., Numao, S., Park, K.H., Withers, S.G. Brayer, G.D. (2005) Acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic α-amylase in complex with analogues and their elongated counterparts. Biochemistry 44, 3347 3357.
10. Machius, M., Vértesy, L., Huber, R. Wiegand, G. (1996) Carbohydrate and protein-based inhibitor of porcine pancreaticα-amylase: structure analysis and comparison of their binding characteristics. J Mol Biol 260, 409 421.
11. Noda, K., Umeda, F. Nawata, H. (1997) Effect of acarbose on glucose intolerance in patients with non-insulin-dependent diabetes mellitus. Diabetes Res Clin Pract 37, 129 136.
12. Qian, M., Haser, R., Buisson, G., Duée, E. Payan, F. (1994) The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2·2 Å resolution. Biochemistry 33, 6284 6294.
13. Qian, M., Nahoum, V., Bonicel, J., Bischoff, H., Henrissat, B. Payan, F. (2001) Enzyme-catalyzed condensation reaction in a mammalian α-amylase. high-resolution structural analysis of an enzyme-inhibitor complex. Biochemistry 40, 7700 7709.
14. Robyt, J.F. French, D. (1970) The action pattern of porcine pancreatic α-amylase in relationship to the substrate binding site of the enzyme. J Biol Chem 245, 3917 3927.
15. Salvatore, T. Giugliano, D. (1996) Pharmacokinetic-pharmacodynamic relationships of acarbose. Clin Pharmacokinet 30, 94 106.
16. Seigner, C., Prodanov, E. Machis-Moren, G. (1987) The determination of subsite binding energies of porcine pancreatic alpha-amylase by comparing hydrolytic activity towards substrates. Biochim Biophys Acta 913, 200 209.
17. Shirling, E.B. Gottlieb, D. (1966) Methods for characterization of Streptomyces species. Int J Syst Bacteriol 16, 313 340.
18. Tatusova, T.A. Madden, T.L. (1999) BLAST 2 sequences, a new tool for comparing protein and nucleotide sequences. FEMS Microbiol Lett 174, 247 250.
19. Truscheit, E., Frommer, W., Junge, B., Müller, L., Schmidt, D.D. Wingeder, W. (1981) Chemie und biochemie. Mikrobieller α-glucosidasen- inhibitoren. Angew Chem, Int Ed Engl 20, 744 761.
20. Williams, S.T., Goodfellow, M., Alderson, G., Wellington, H., Sneath, A. Sackin, M.J. (1983) Numerical classification of Streptomyces and related genera. J Gen Microbiol 129, 1743 1813.
21. IV-α-maltododecaosyl analogues. Carbohydr Res 338, 1969 1980.