Literature DB >> 1717694

Mutational analysis of the structure and function of the adenine phosphoribosyltransferase enzyme of Chinese hamster.

J G de Boer1, B W Glickman.   

Abstract

We have analyzed the adenine phosphoribosyltransferase (APRT) enzyme from Chinese hamster ovary cells through the study of mutants that are able to grow in the presence of the toxic adenine analogue 8-azaadenine. The distribution of the amino acid alterations was analyzed in terms of the binding regions for the purine and phosphoribosylpyrophosphate substrates and a comparison was made with mutants known in human APRT and human, mouse and hamster hypoxanthine-guanine phosphoribosyltransferase. A number of mutants were found to cluster in several regions of the amino acid sequence. Residual enzyme activity with adenine was determined and this was correlated with substrate binding regions. A model of the secondary structure features is proposed.

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Year:  1991        PMID： 1717694     DOI： 10.1016/0022-2836(91)80212-d

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


  8 in total

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7.  Influence of alkyltransferase activity and chromosomal locus on mutational hotspots in Chinese hamster ovary cells.

Authors:  A Belouchi; M Ouimet; P Dion; N Gaudreault; W E Bradley
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8.  Correction of a deletion mutant by gene targeting with an adenovirus vector.

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  8 in total

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