Aminopeptidase N from Escherichia coli. Unusual Interactions with the Cell Surface
نویسندگان
چکیده
منابع مشابه
Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250.
Aminopeptidase N (APN; EC 3.4.11.2) purified from Escherichia coli has been crystallized with the optically pure aminophosphinic inhibitor PL250, H(3)N(+)-CH(CH(3))-P(O)(OH)-CH(2)-CH(CH(2)Ph)-CONH-CH(CH(2)Ph)CO(2)(-), which mimics the transition state of the hydrolysis reaction. PL250 inhibits APN with a K(i) of 1.5-2.2 nM and its three-dimensional structure in complex with E. coli APN showed i...
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F4(+) enterotoxigenic Escherichia coli (ETEC) strains cause diarrheal disease in neonatal and post-weaned piglets. Several different host receptors for F4 fimbriae have been described, with porcine aminopeptidase N (APN) reported most recently. The FaeG subunit is essential for the binding of the three F4 variants to host cells. Here we show in both yeast two-hybrid and pulldown assays that APN...
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Phage T6 was used as a label to follow the growth of the outer membrane in a strain of Escherichia coli temperature sensitive for the production of the T6 receptor. Extension of the surface takes place at the cell poles. Small cells extend at only one pole, whereas larger cells grow from both poles. The change from unipolar to bipolar growth appears to depend on the attainment of a particular c...
متن کاملPurification and Properties of an Aminopeptidase from Escherichia coli*
An aminopeptidase from Escherichia coli has been purified to homogeneity and crystallized. This peptidase is responsible for about 65% of the hydrolytic activity found in crude extracts toward the substrate methionylalanylserine. It resembles the so-called leucine arninop!ptidase of hog kidney in several respects, including size, metal requirements, and peptide specificity. Evidence based on su...
متن کاملPurification and properties of an aminopeptidase from Escherichia coli.
An aminopeptidase from Escherichia coli has been purified to homogeneity and crystallized. This peptidase is responsible for about 65% of the hydrolytic activity found in crude extracts toward the substrate methionylalanylserine. It resembles the so-called leucine arninop!ptidase of hog kidney in several respects, including size, metal requirements, and peptide specificity. Evidence based on su...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1977
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1977.tb11408.x