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Small-molecule metabolism: an enzyme mosaic
Authors:Sarah A Teichmann  Stuart C G Rison  Janet M Thornton  Monica Riley  Julian Gough  Cyrus Chothia
Institution:

a Dept of Biochemistry and Molecular Biology, University College London, Darwin Building, Gower Street, London, UK WC1E 6BT

b Josephine Bay Paul Centre for Comparative Molecular Biology and Evolution, 7 MBL St, Woods Hole, MA 02543-1015, USA

c MRC Laboratory of Molecular Biology, Hills Road, Cambridge, UK CB2 1TQ

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 not, vert, similar90% 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:evolution  metabolic pathways  enzymes  Escherichia coli  protein families
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