PUMA publications for /user/siemannherzberg/zincThu Jan 25 13:38:08 CET 2018{PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS}{JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC}{SEP 15}{3rd International Symposium on Biocatalysis and Biotransformations
(BIOTRANS 97), LA GRANDE MOTTE, FRANCE, SEP 22-26, 1997}{1-4, SI}{367-370}{The hydantoin amidohydrolase from Arthrobacter aurescens DSM 3745 is a
zinc metalloenzyme}{Article; Proceedings Paper}{5}{1998}Arthrobacter amidase; aurescens; metalloenzyme} myown zinc {hydantoinase; {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.}