The hydantoin amidohydrolase (hydantoinase) from Arthrobacter aurescens
DSM 3745 was purified to homogeneity and subjected to metal analysis
under atomic absorption spectrometry (AAS) and inductive coupled
plasma-atomic emission spectrometry (ICP-AES). Three independent
preparations of homogeneous enzyme indicated that 1 mol of the active
enzyme contains 10 mol zinc ions. This corresponds to 2.5 mol zinc per
mol subunit, since the hydantoinase consists of four identical subunits.
Only trace amounts of manganese, magnesia, nickel and cobalt were
detected. Other metals were either absent or existed below detection
levels. (C) 1998 Elsevier Science B.V. All rights reserved.
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