Title of article :
Small-molecule metabolism: an enzyme mosaic
Author/Authors :
Cyrus Chothia and Sarah A. Teichmann، نويسنده , , Stuart C.G. Rison، نويسنده , , Christine A. Orengo and Janet M. Thornton، نويسنده , , Monica Riley، نويسنده , , Julian Gough and Cyrus Chothia، نويسنده , , Cyrus Chothia، نويسنده ,
Issue Information :
ماهنامه با شماره پیاپی سال 2001
Pages :
5
From page :
482
To page :
486
Abstract :
Escherichia coli has been a popular organism for studying metabolic pathways. In an attempt to find out more about how these pathways are constructed, the enzymes were analysed by defining their protein domains. Structural assignments and sequence comparisons were used to show that 213 domain families constitute ∼90% of the enzymes in the small-molecule metabolic pathways. Catalytic or cofactor-binding properties between family members are often conserved, while recognition of the main substrate with change in catalytic mechanism is only observed in a few cases of consecutive enzymes in a pathway. Recruitment of domains across pathways is very common, but there is little regularity in the pattern of domains in metabolic pathways. This is analogous to a mosaic in which a stone of a certain colour is selected to fill a position in the picture.
Keywords :
Metabolic pathways , Protein families , Escherichia coli , Enzymes , Evolution
Journal title :
Trends in Biotechnology
Serial Year :
2001
Journal title :
Trends in Biotechnology
Record number :
1232646
Link To Document :
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