General Screening of Enzyme Inhibitors

Tanaka, Haruo; Kawakita, Kazuhito; Imamura, Nobutaka; Tsuzuki, Kazuo; Shiomi, Kazuro

doi:10.1007/978-1-4612-4412-7_7

Cited by 5 publications

(3 citation statements)

References 230 publications

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“…Ubenimex (bestatin), an inhibitor of arginyl aminopeptidase (aminopeptidase B) and leucyl aminopeptidase, was obtained from cultures of Streptomyces olivoreticuli. It has a number of physiological activities, and in combination with other therapy has been used in Japan since 1987 to treat nonlymphocytic leukemia [57]. Since many of the ß-lactam antibiotics are susceptible to the hydrolytic activity of ß-lactamases, inhibitors of the latter enzyme are valuable and are administered in conjunction with the antibiotic itself.…”

Section: Useful Physiological Activities From Microorganismsmentioning

confidence: 99%

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Microbial Secondary Metabolites Play Important Roles in Medicine; Prospects for Discovery of New Drugs

Bentley

1997

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Section: Useful Physiological Activities From Microorganismsmentioning

confidence: 99%

“…More than 150 secondary metabolites have such properties, and some are used to treat human conditions [57] . Lovostatin (mevinolin) was originally isolated from Monascus rubrum and Aspergillus terreus as an antibiotic, but it is now widely prescribed as an antihypercholesterolemic medication.…”

Section: Useful Physiological Activities From Microorganismsmentioning

confidence: 99%

Microbial Secondary Metabolites Play Important Roles in Medicine; Prospects for Discovery of New Drugs

Bentley

1997

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“…The results of some of these types of screening methods developed in our group have been reviewed previously. 42) , 43) …”

Section: Screening For Enzyme Inhibitorsmentioning

confidence: 99%

Cell-based screening strategy in the search for bioactive microbial secondary metabolites

Iwasaki

Ōmura

2004

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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(Contributed by Satoshi 1MURA, M. J. A., Feb. 12, 2004) Abstract: Here we present results obtained in our group from cell-based screenings of microbial secondary metabolites using intact microbial and mammalian cells having specific functions. We present summaries of the following five categories of compounds and the strategies that were used to identify them. (1) Antibacterial agents targeting cell wall peptidoglycan synthesis as well as active agents against organisms other than bacteria were identified by a combination of Bacillus subtilis and Mycoplasma as test organisms. (2) Antimetabolites, such as herbicidal agents targeting glutamine synthase, were identified using B. subtilis grown on minimal medium with or without the addition of glutamine and folate inhibitors by combination of B. subtilis and Enterococcus faecium, which have distinct folate metabolic pathways. (3) Among inhibitors of lipid metabolism, acyl-CoA synthetase inhibitors were identified using two mutants of C. lipolytica with different deletion sites in the fatty acid metabolic pathways, HMG-CoA synthase inhibitors were identified using Vero cells cultured in the presence and absence of mevalonate, and anti-atherosclerosis agents were identified using macrophages. (4) IL-6 inhibitors were detected by a combination of IL-6-dependent and independent murine hybridoma MH60 cells, and (5) Small molecules with TNF-like activities were identified using a mouse neuroblastoma cell line. Some advantages of such screening method and the significance of the identified compounds are discussed.

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Isolation of cathepsin B inhibitory peptides, Cabin-A1 and -A2, from a tryptic and chymotryptic hydrolysate of human serum albumin

et al. 2002

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General Screening of Enzyme Inhibitors

Cited by 5 publications

References 230 publications

Microbial Secondary Metabolites Play Important Roles in Medicine; Prospects for Discovery of New Drugs

Microbial Secondary Metabolites Play Important Roles in Medicine; Prospects for Discovery of New Drugs

Cell-based screening strategy in the search for bioactive microbial secondary metabolites

Isolation of cathepsin B inhibitory peptides, Cabin-A1 and -A2, from a tryptic and chymotryptic hydrolysate of human serum albumin

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