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The hydantoin amidohydrolase from Arthrobacter aurescens DSM 3745 is a zinc metalloenzyme

, , , und . JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 5 (1-4, SI): 367-370 (September 1998)3rd International Symposium on Biocatalysis and Biotransformations (BIOTRANS 97), LA GRANDE MOTTE, FRANCE, SEP 22-26, 1997.

Zusammenfassung

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.

Links und Ressourcen

DOI:
10.1016/S1381-1177(98)00060-5
URL:
BibTeX-Schlüssel:
ISI:000076071300066
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