%0 Journal Article %1 ISI:000074643300006 %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; cyclic metalloenzyme; myown zinc} {hydantoinase; %N 4 %P 211-218 %R 10.1016/S1381-1177(97)00038-6 %T Catalytic and structural function of zinc for the hydantoinase from Arthrobacter aurescens DSM 3745 %U https://doi.org/10.1016/S1381-1177(97)00038-6 %V 4 %X Metal dependency of the hydantoin amidohydrolase (hydantoinase) from Arthrobacter aurescens DSM 3745 has been analyzed based on kinetic studies of metal/chelator-caused enzyme inactivation, denaturation and reactivation, accompanied by the identification of specific metal binding ligands. The enzyme can be inactivated by metal chelating agents and-apart from the loss of its activity-completely dissociates into its subunits. Enzyme activity can be restored from recollected monomers by the addition of cobalt, manganese or zinc-ions, whereas nickel and magnesia remain ineffective. Subjection of the hydantoinase to metal analysis reveals a content of 10 mol zinc per mol enzyme. Zinc plays an essential role not only for the catalytic activity but also for the stabilization of the active quarternary structure of the hydantoinase. Histidine-specific chemical modification of the enzyme causes a complete loss of the catalytic activity and reveals histidine residues as putative zinc binding ligands. Both, the metal/chelator-caused enzyme inactivation as well as the metal-caused enzyme reactivation, can be reduced in the presence of the substrate. Therefore, it is very likely that at least one metal-ion acts specifically near or at the active site of the enzyme. (C) 1998 Elsevier Science B.V. All rights reserved.

@article{ISI:000074643300006, abstract = {{Metal dependency of the hydantoin amidohydrolase (hydantoinase) from Arthrobacter aurescens DSM 3745 has been analyzed based on kinetic studies of metal/chelator-caused enzyme inactivation, denaturation and reactivation, accompanied by the identification of specific metal binding ligands. The enzyme can be inactivated by metal chelating agents and-apart from the loss of its activity-completely dissociates into its subunits. Enzyme activity can be restored from recollected monomers by the addition of cobalt, manganese or zinc-ions, whereas nickel and magnesia remain ineffective. Subjection of the hydantoinase to metal analysis reveals a content of 10 mol zinc per mol enzyme. Zinc plays an essential role not only for the catalytic activity but also for the stabilization of the active quarternary structure of the hydantoinase. Histidine-specific chemical modification of the enzyme causes a complete loss of the catalytic activity and reveals histidine residues as putative zinc binding ligands. Both, the metal/chelator-caused enzyme inactivation as well as the metal-caused enzyme reactivation, can be reduced in the presence of the substrate. Therefore, it is very likely that at least one metal-ion acts specifically near or at the active site of the enzyme. (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/217f39463dc8fd94d2571edbed22eb8bb/siemannherzberg}, da = {{2018-01-25}}, doc-delivery-number = {{ZY634}}, doi = {{10.1016/S1381-1177(97)00038-6}}, interhash = {e8f9253b7f1f51aad7f025bc46340ffc}, intrahash = {17f39463dc8fd94d2571edbed22eb8bb}, issn = {{1381-1177}}, journal = {{JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC}}, journal-iso = {{J. Mol. Catal. B-Enzym.}}, keywords = {Arthrobacter amidase; aurescens; cyclic metalloenzyme; myown zinc} {hydantoinase;}, keywords-plus = {{5,6-DIHYDROPYRIMIDINE AMIDOHYDROLASE; PURIFICATION; ENZYME; PSEUDOMONAS-PUTIDA-77; BIOLOGY; LIVER}}, language = {{English}}, month = {{JUN 14}}, number = {{4}}, number-of-cited-references = {{21}}, pages = {{211-218}}, publisher = {{ELSEVIER SCIENCE BV}}, research-areas = {{Biochemistry \& Molecular Biology; Chemistry}}, times-cited = {{24}}, timestamp = {2018-01-25T12:38:18.000+0100}, title = {{Catalytic and structural function of zinc for the hydantoinase from Arthrobacter aurescens DSM 3745}}, type = {{Article}}, unique-id = {{ISI:000074643300006}}, url = {https://doi.org/10.1016/S1381-1177(97)00038-6}, usage-count-last-180-days = {{0}}, usage-count-since-2013 = {{2}}, volume = {{4}}, web-of-science-categories = {{Biochemistry \& Molecular Biology; Chemistry, Physical}}, year = {{1998}} }