The thiolase superfamily: condensing enzymes with diverse reaction specificities
| Autor: | Rik K. Wierenga, Gitte Meriläinen, Antti M. Haapalainen |
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| Rok vydání: | 2006 |
| Předmět: |
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Molecular chemistry.chemical_classification Protein Conformation Thiolase Stereochemistry Thiosulfates Biology Condensation reaction Biochemistry Catalysis Protein Structure Secondary Substrate Specificity Kinetics Polyketide Residue (chemistry) Protein structure Enzyme chemistry Catalytic cycle Animals Humans Molecular Biology Acyltransferases Cysteine |
| Zdroj: | Trends in Biochemical Sciences. 31:64-71 |
| ISSN: | 0968-0004 |
| DOI: | 10.1016/j.tibs.2005.11.011 |
| Popis: | The formation of a carbon-carbon bond is an essential step in the biosynthetic pathways by which fatty acids and polyketides are made. The thiolase superfamily enzymes catalyse this carbon-carbon-bond formation via a thioester-dependent Claisen-condensation-reaction mechanism. In this way, fatty-acid chains and polyketides are made by sequentially adding simple building blocks, such as acetate units, to the growing molecule. A common feature of these enzymes is a reactive cysteine residue that is transiently acylated in the catalytic cycle. The wide catalytic diversity of the thiolase superfamily enzymes is of great interest. In particular, the type-III polyketide synthases make complicated compounds of great biological importance using multiple, subsequent condensation reactions, which are all catalysed in the same active-site cavity. The crucial metabolic importance of the bacterial fatty-acid-synthesizing enzymes stimulates in-depth studies that aim to develop efficient anti-bacterial drugs. |
| Databáze: | OpenAIRE |
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