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Purification and properties of α‐amino‐ϵ‐caprolactam racemase from Achromobacter obae
Author(s) -
Ahmed Syed Ashrafuddin,
Esaki Nobuyoshi,
Soda Kenji
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80770-9
Subject(s) - chemistry , achromobacter , pyridoxal , chromatography , caprolactam , sedimentation coefficient , sepharose , enzyme , sodium dodecyl sulfate , biochemistry , organic chemistry , pseudomonas , biology , bacteria , genetics
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.