Abstract
3-Ketovalidoxylamine A C–N lyase is one of three key enzymes in the production of valienamine, which is a potent glucosidase inhibitor from validamycin A. N-p-Nitrophenyl-3-ketovalidamine, used as the substrate of 3-ketovalidoxylamine A C–N lyase, was prepared from N-p-nitrophenylvalidamine with free cells of Stenotrophomonasmaltrophilia CCTCC M 204024. The yield and selectivity of N-p-nitrophenyl-3-ketovalidamine from cells were improved by treatment with 10 mM ethylenediaminetetraacetic acid. The optimal pH and temperature for N-p-nitrophenyl-3-ketovalidamine formation was pH 6.0 and 30°C, respectively. N-p-Nitrophenyl-3-ketovalidamine was formed with a yield of 0.68 in the first batch.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Asano N, Takeuchi M, Ninomiya K, Kameda Y, Matsui K (1984) Microbial degradation of validamycin A by Flavobacterium saccharophilum: enzyme cleavage of C–N linkage in validoxylamine A. J Antibiot 37:859–867
Asano N, Takeuchi M, Ninomiya K, Kameda Y, Matsui K (1989) Preparation of 3-amino-3 deoxy derivatives of trehalose and sucrose and their activities. J Antibiot 42:585–590
Chen XL, Fan YX, Zheng YG, Shen YC (2003) Properties and production of valienamine and its related analogues. Chem Rev 103:1955–1977
Hayano K, Fukui S (1967) Purification and properties of 3-ketosucrose-forming enzyme from the cells of Agrobacterium tumefaciens. J Biol Chem 242:3655–3672
Kameda Y, Asano N, Yoshikawa M, Matsui K (1980) Valienamine as an α-glucosidase inhibition. J Antibiot 33:1575–1576
Kameda Y, Asano N, Yoshikawa M, Takeuchi M, Yamaguchi T, Matsui K (1984) Valiolamine, a new α-glucosidase inhibiting aminocyclitol produced by Streptomyces hygroscopicus. J Antibiot 37:1301–1307
Maeda A, Adachi S, Matsuno R (2001) Improvement of selectivity in 3-ketocellobiose production from cellobiose by Agrobacterium tumefaciens. Biochem Eng J 8:217–221
Maeda A, Kataoka H, Adachi S, Matsuno R (2003) Transformation of cellobiose to 3-ketocellobiose by the EDTA-treated Agrobacterium tumefaciens cells. J Biosci Bioeng 95:608–611
Pietsch M, Walter M, Buchholz K (1994) Regioselective synthesis of new sucrose derivatives via 3-ketosucrose. Carbohydr Res 254:183–194
Sode K, Akaike E, Sugiura H, Tsugawa W (2001) Enzymatic synthesis of a novel trehalose derivative, 3,3′-diketotrehalose, and its potential application as the trehalose enzyme inhibitor. FEBS Lett 489:42–45
Stoppok E, Walter J, Buchholz K (1995) The effect of pH and oxygen concentration on the formation of 3-ketodisaccharides by Agrobacterium tumefaciens. Appl Microbiol Biotechnol 43:706–712
Takeuchi M, Asano N, Kameda Y, Matsui K (1985) Purification and properties of 3-ketovalidoxylamine A C–N lyase from Flavobacterium saccharophilum. J Biochem 98:1631–1638
Takeuchi M, Ninomiya K, Kawabata K, Asano N, Kameda Y, Matsui K (1986) Purification and properties of glucoside 3-dehydrogenase from Flavobacterium saccharophilum. J Biochem 100:1049–1055
Takeuchi M, Asano N, Kameda Y, Matsui K (1988) Purification and properties of soluble d-glucoside 3-dehydrogenase from Flavobacterium saccharophilum. Agric Biol Chem 52:1905–1912
Zhang JF, Zheng YG, Shen YC (2006) Purification and characterization of the glucoside 3-dehydrogenase produced by a newly isolated Stenotrophomonas maltrophilia CCTCC M 204024. Appl Microbiol Biotechnol 71:638–645
Zheng YG, Jin LQ, Shen YC (2004) Resin-catalyzed degradation of validamycin A for production of validoxylamine A. Catal Commun 5:519–525
Zheng YG, Shentu XP, Shen YC (2005a) Inhibition of porcine small intestinal sucrase by valienamine. J Enzyme Inhib Med Chem 20:49–53
Zheng YG, Zhang XF, Shen YC (2005b) Microbial transformation of validamycin A to valienamine by immobilized cells. Biocatal Biotransform 23:71–77
Zheng YG, Xue YP, Shen YC (2006) Production of valienamine by a newly isolated strain: Stenotrophomonas maltrophilia. Enzyme Microb Technol 39:1060–1065
Acknowledgements
This work was supported by the National Fund of the Major Basic Research Development Program 973 of China (2003CB716005), the National Natural Science Foundation of China (20176055), and the Natural Science Foundation of Zhejiang Province (Y305242).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Zhang, JF., Zheng, YG., Liu, ZQ. et al. Preparation of 3-ketovalidoxylamine A C–N lyase substrate: N-p-nitrophenyl-3-ketovalidamine by Stenotrophomonas maltrophilia CCTCC M 204024. Appl Microbiol Biotechnol 73, 1275–1281 (2007). https://doi.org/10.1007/s00253-006-0619-8
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00253-006-0619-8