Expression in Escherichia coli of a clavaminic acid synthase isozyme: A trifunctional oxygenase involved in clavulanic acid biosynthesis
β Scribed by Elizabeth J. Lawlor; Stephen W. Elson; Susan Holland; Robert Cassels; John E. Hodgson; Matthew D. Lloyd; Jack E. Baldwin; Christopher J. Schofield
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- French
- Weight
- 851 KB
- Volume
- 50
- Category
- Article
- ISSN
- 0040-4020
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β¦ Synopsis
purification and sequencing of clavaminic acid synthase (CAS) activities from S. cluvuligerus SC2 pxovided evidence for the existence of two CAS i.wzymes. One of these isozymes was cloned aad expressed in E. COIL The recombiaaat CAS isozyme was shown to catalyse the hydroxylation of (2S)-5-guanidmo-2-(2'-oxoazetidin-l'-yl)pentanoic acid, in addition to the pmduction of clavaminic acid from dihydmclavamiaic acid via proclavaminic acid, consistent with the hifanctional role proposed for clavaminic acid syathase in the biosynthesis of clavulanii acid. A preliminary pmifiiatioa and character&km of the recombinant isozyme is reported
π SIMILAR VOLUMES
## Abstract Lβamino acid deaminases catalyze the deamination of natural Lβamino acids. Two types of Lβamino acid deaminase have been identified in __Proteus__ species. One exhibits high levels of activity toward a wide range of aliphatic and aromatic Lβamino acids, typically Lβphenylalanine, wherea