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Small-molecule metabolism: an enzyme mosaic
- Source :
- Trends in Biotechnology. 19:482-486
- Publication Year :
- 2001
- Publisher :
- Elsevier BV, 2001.
-
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 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.
- Subjects :
- Protein family
Protein domain
Coenzymes
Sequence Homology
Bioengineering
Biology
medicine.disease_cause
Substrate Specificity
Evolution, Molecular
Protein structure
Pyruvic Acid
Escherichia coli
medicine
Organism
Fucose
Genetics
chemistry.chemical_classification
Binding Sites
Nucleotides
Mechanism (biology)
Tryptophan
Nucleosides
Enzymes
Protein Structure, Tertiary
Metabolic pathway
Pyrimidines
Enzyme
chemistry
Purines
Biotechnology
Subjects
Details
- ISSN :
- 01677799
- Volume :
- 19
- Database :
- OpenAIRE
- Journal :
- Trends in Biotechnology
- Accession number :
- edsair.doi.dedup.....9ce07d4515cf30b38583d8a04cae8701
- Full Text :
- https://doi.org/10.1016/s0167-7799(01)01813-3