Small Molecule Metabolism: An Enzyme Mosaic

S.A. Teichmann, S. C. G. Rison, J. M. Thornton, M. Riley, J. Gough, C. Chothia

Research output: Contribution to journalArticle (Academic Journal)peer-review

51 Citations (Scopus)


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 approximately 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.
Translated title of the contributionSmall Molecule Metabolism: An Enzyme Mosaic
Original languageEnglish
Article number482-486
JournalTrends Biotechnol
Volume19 (12)
Publication statusPublished - 2001

Bibliographical note

Other identifier: 1040028


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