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Expression in Escherichia coli of a clavaminic acid synthase isozyme: A trifunctional oxygenase involved in clavulanic acid biosynthesis

✍ 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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✦ 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


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## Abstract L‐amino acid deaminases catalyze the deamination of natural L‐amino acids. Two types of L‐amino acid deaminase have been identified in __Proteus__ species. One exhibits high levels of activity toward a wide range of aliphatic and aromatic L‐amino acids, typically L‐phenylalanine, wherea