Literature DB >> 6383377

E. coli aspartokinase II-homoserine dehydrogenase II polypeptide chain has a triglobular structure.

J Belfaiza, A Fazel, K Müller, G N Cohen.   

Abstract

E.coli aspartokinase II-homoserine dehydrogenase II is, as aspartokinase I-homoserine dehydrogenase I, composed of three globular domains: the N-terminal domain is endowed with kinase activity; the C-terminal domain carries the dehydrogenase activity. These two parts of the polypeptide chain are separated by a central inactive domain. Thus, the polypeptide chains of the two multifunctional proteins are homologous not only in their sequence but also in their triglobular domain structure.

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Year:  1984        PMID: 6383377     DOI: 10.1016/0006-291x(84)90373-5

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  Molecular genetics of the maize (Zea mays L.) aspartate kinase-homoserine dehydrogenase gene family.

Authors:  G J Muehlbauer; D A Somers; B F Matthews; B G Gengenbach
Journal:  Plant Physiol       Date:  1994-12       Impact factor: 8.340

  1 in total

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