%0 Journal Article %1 ISI:000076071300066 %A May, O %A Siemann, M %A Siemann, MG %A Syldatk, C %C PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS %D 1998 %I ELSEVIER SCIENCE BV %J JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC %K Arthrobacter amidase; aurescens; metalloenzyme} myown zinc {hydantoinase; %N 1-4, SI %P 367-370 %R 10.1016/S1381-1177(98)00060-5 %T The hydantoin amidohydrolase from Arthrobacter aurescens DSM 3745 is a zinc metalloenzyme %U https://doi.org/10.1016/S1381-1177(98)00060-5 %V 5 %X 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.

@article{ISI:000076071300066, abstract = {{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.}}, added-at = {2018-01-25T13:38:08.000+0100}, address = {{PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS}}, affiliation = {{Siemann, M (Reprint Author), Univ Stuttgart, Inst Bioverfahrenstech, Allmandring 31, D-70569 Stuttgart, Germany. Univ Stuttgart, Inst Bioverfahrenstech, D-70569 Stuttgart, Germany. Tech Univ Clausthal, Inst Mineral, Abt Geochem, D-38678 Clausthal Zellerfeld, Germany.}}, author = {May, O and Siemann, M and Siemann, MG and Syldatk, C}, biburl = {https://puma.ub.uni-stuttgart.de/bibtex/20033cb539dc528c3e21a8b9bab8ccf2e/siemannherzberg}, da = {{2018-01-25}}, doc-delivery-number = {{122KT}}, doi = {{10.1016/S1381-1177(98)00060-5}}, interhash = {0e0c6a982c0e44086548d8e967cc2d52}, intrahash = {0033cb539dc528c3e21a8b9bab8ccf2e}, issn = {{1381-1177}}, journal = {{JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC}}, journal-iso = {{J. Mol. Catal. B-Enzym.}}, keywords = {Arthrobacter amidase; aurescens; metalloenzyme} myown zinc {hydantoinase;}, keywords-plus = {{PURIFICATION; BIOLOGY; ENZYME; LIVER}}, language = {{English}}, month = {{SEP 15}}, note = {{3rd International Symposium on Biocatalysis and Biotransformations (BIOTRANS 97), LA GRANDE MOTTE, FRANCE, SEP 22-26, 1997}}, number = {{1-4, SI}}, number-of-cited-references = {{13}}, pages = {{367-370}}, publisher = {{ELSEVIER SCIENCE BV}}, research-areas = {{Biochemistry \& Molecular Biology; Chemistry}}, times-cited = {{12}}, timestamp = {2018-01-25T12:38:18.000+0100}, title = {{The hydantoin amidohydrolase from Arthrobacter aurescens DSM 3745 is a zinc metalloenzyme}}, type = {{Article; Proceedings Paper}}, unique-id = {{ISI:000076071300066}}, url = {https://doi.org/10.1016/S1381-1177(98)00060-5}, usage-count-last-180-days = {{0}}, usage-count-since-2013 = {{1}}, volume = {{5}}, web-of-science-categories = {{Biochemistry \& Molecular Biology; Chemistry, Physical}}, year = {{1998}} }