Medium- and short-chain dehydrogenase/reductase gene and protein families
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A frame that forgets how it found something cannot be audited. These are the routes that admitted this work.
No Canadian affiliation. An affiliation-only frame — the usual design — would never have seen this work. It is one of the works that make the case for inverting the frame.
Abstract
Short-chain dehydrogenases/reductases (SDRs) constitute a large family of NAD(P)(H)-dependent oxidoreductases, sharing sequence motifs and displaying similar mechanisms. SDR enzymes have critical roles in lipid, amino acid, carbohydrate, cofactor, hormone and xenobiotic metabolism as well as in redox sensor mechanisms. Sequence identities are low, and the most conserved feature is an alpha/beta folding pattern with a central beta sheet flanked by 2 - 3 alpha-helices from each side, thus a classical Rossmannfold motif for nucleotide binding. The conservation of this element and an active site, often with an Asn-Ser-Tyr-Lys tetrad, provides a platform for enzymatic activities encompassing several EC classes, including oxidoreductases, epimerases and lyases. The common mechanism is an underlying hydride and proton transfer involving the nicotinamide and typically an active site tyrosine residue, whereas substrate specificity is determined by a variable C-terminal segment. Relationships exist with bacterial haloalcohol dehalogenases, which lack cofactor binding but have the active site architecture, emphasizing the versatility of the basic fold in also generating hydride transfer-independent lyases. The conserved fold and nucleotide binding emphasize the role of SDRs as scaffolds for an NAD(P)(H) redox sensor system, of importance to control metabolic routes, transcription and signalling.
Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.
The record
- Venue
- Cellular and Molecular Life Sciences
- Topic
- Enzyme Structure and Function
- Field
- Materials Science
- Canadian institutions
- —
- Funders
- VetenskapsrådetKnut och Alice Wallenbergs StiftelseKarolinska InstitutetStiftelsen för Strategisk ForskningNovo NordiskOntario Genomics InstituteOntario GenomicsGenome CanadaOntario Innovation TrustWellcome TrustGlaxoSmithKline
- Keywords
- BiochemistryCofactorNAD+ kinaseBiologyActive siteDehydrogenaseBinding siteSequence motifConsensus sequenceOxidoreductaseConserved sequenceWalker motifsPeptide sequenceNucleotideEnzymeChemistryStereochemistryGene
- Has abstract in OpenAlex
- yes