Relevant articles and documents
Deracemization of unnatural amino acid: Homoalanine using d-amino acid oxidase and ω-transaminase
Seo, Young-Man Mathew, Sam Bea, Han-Seop Khang, Yong-Ho Lee, Sang-Hyeup Kim, Byung-Gee Yun, Hyungdon
A deracemization method was developed to generate optically pure l-homoalanine from racemic homoalanine using d-amino acid oxidase and ω-transaminase. A whole cell reaction using a biphasic system converted 500 mM racemic homoalanine to 485 mM l-homoalanine (>99% ee). The Royal Society of Chemistry 2012.
Synthesis of 4-hydroxyisoleucine by the aldolase-transaminase coupling reaction and basic characterization of the aldolase from Arthrobacter simplex AKU 626
Ogawa, Jun Yamanaka, Hiroyuki Mano, Junichi Doi, Yuko Horinouchi, Nobuyuki Kodera, Tomohiro Nio, Noriki Smirnov, Sergey V. Samsonova, Natalya N. Kozlov, Yury I. Shimizu, Sakayu
Arthrobacter simplex AKU 626 was found to synthesize 4-hydroxyisoleucine from acetaldehyde, α-ketobutyrate, and L-glutamate in the presence of Escherichia coli harboring the branched chain amino acid transaminase gene (ilvE) from E. coli K12 substrain MG-1655. By using resting cells of A. simplex AKU 626 and E. coli BL21(DE3)/pET-15b-ilvE, 3.2 mM 4-hydroxyisoleucine was produced from 250 mM acetaldehyde, 75 mM α-ketobutyrate, and 100mM L-glutamate with a molar yield to α-ketobutyrate of 4.3% in 50 mM Tris-HCl buffer (pH 7.5) containing 2 mM MnCl2·4H2O at 28°C for 2 h. An aldolase that catalyzes the aldol condensation of acetaldehyde and α-ketobutyrate was purified from A. simplex AKU 626. Mn2+ and pyridoxal 5′-monophosphate were effective in stabilizing the enzyme. The native and subunit molecular masses of the purified aldolase were about 180 and 32 kDa respectively. The N-terminal amino acid sequence of the purified enzyme showed no significant homology to known aldolases.
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