Purification and properties of α‐amino‐ϵ‐caprolactam racemase from Achromobacter obae
Authors:
- Syed Ashrafuddin AhmedSASyed Ashrafuddin Ahmed
- Nobuyoshi EsakiNENobuyoshi Esaki
- Kenji SodaKSKenji Soda
- 27 December 1982
- journal article
- Published by Wiley in FEBS Letters
- Vol. 150 (2) , 370-374
Abstract
We have purified a unique enzyme, α‐amino‐ϵ‐caprolactam racemase 945‐fold from an extract of Achromobacter obae by Octyl—Sepharose CL‐4B and Thiopropyl—Sepharose 6B and some other chromatographies. The purified enzyme was found homogeneous by sodium dodecyl sulfate—polyacrylamide gel electrophoresis and analytical ultracentrifugation. The enzyme has a monomeric structure with M r ∼ 50 000 and a sedimentation coefficient (s 20,w) of 4.28 S. The enzyme contains pyridoxal 5'‐phosphate as a coenzyme. The pH optimum for the enzyme activity is ∼9.0. D‐ and L‐α‐amino‐ϵ‐caprolactams are the only substrates. The K m values for the D‐ and L‐isomers are, 8 and 6 mM, respectively.Keywords
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