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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Belactins A and B, new serine carboxypeptidase inhibitors produced by Actinomycete. II. Physico-chemical properties, structure determinations and enzymatic inhibitory activities compared with other beta-lactone containing inhibitors.

Belactins A and B, new inhibitors of serine carboxypeptidase were discovered in the fermentation broth of Saccharopolyspora sp. MK19-42F6. The structures of belactins A and B were determined to be 4-[3-[(2-amino-5-chlorobenzoyl)amino]-1,1-dimethyl-2-oxobutyl]-3- methyl-2-oxetanone and 4-[3-[[2-(beta-glucopyranosylamino)-5-chlorobenzoyl]amino]-1,1- dimethyl-2-oxobutyl]-3-methyl-2-oxetanone respectively by various spectral analyses. Belactins A and B do not inhibit esterase or lipase at 100 micrograms/ml but have more specific inhibitory activities towards carboxypeptidase Y (CP-Y) compared with other beta-lactone-containing inhibitors, such as ebelactones A, B and esterastin.[1]

References

  1. Belactins A and B, new serine carboxypeptidase inhibitors produced by Actinomycete. II. Physico-chemical properties, structure determinations and enzymatic inhibitory activities compared with other beta-lactone containing inhibitors. Murakami, S., Takahashi, Y., Naganawa, H., Takeuchi, T., Aoyagi, T. J. Enzym. Inhib. (1995) [Pubmed]
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