Harold Moellering

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The three-dimensional crystal structure of creatine amidinohydrolase (creatinase EC 3.5.3.3) from Pseudomonas putida, a dimeric enzyme with a molecular weight of 97,000, has been determined by multiple isomorphous replacement, averaging over the local dyad and restrained crystallographic refinement at 1.9 A with a crystallographic R-value of 17.7%. The(More)
N-carbamoylsarcosine amidohydrolase from Arthrobacter sp., a tetramer of polypeptides with 264 amino acid residues each, has been crystallized and its structure solved and refined at 2.0 A resolution, to a crystallographic R-factor of 18.6%. The crystals employed in the analysis contain one tetramer of 116,000 M(r) in the asymmetric unit. The structure(More)
Crystal structures of the enzyme creatine amidinohydrolase (creatinase, EC 3.5.3.3) with two different inhibitors, the reaction product sarcosine and the substrate creatine, bound have been analyzed by X-ray diffraction methods. With the inhibitor carbamoyl sarcosine, two different crystal forms at different pH values have been determined. An enzymatic(More)
Kort & Matrikelstyrelsen, Rentemestervej 8, Copenhagen, DK-2400 NV, Denmark. Department of Geography, Ohio State University, Columbus, OH, 43210, USA National Commission of the SDI of Cuba, Calle 6 No. 301 Esq. 3ra, Miramar, La Habana 11300, Cuba Logistics and Quantitative Methods, CSIR, PO Box 395, Pretoria, 0001, South Africa Department of Geomatics,(More)
Creatinase (creatine amidinohydrolase, EC 3.5.3.3), a homodimer of 45 kDa subunit molecular mass, shows only limited functional stability, and is inaccessible to reconstitution after preceding deactivation, denaturation and dissociation. The enzyme has been characterized regarding its native and denatured states. Studying its unfolding characteristics in(More)
In the analogue era, concern for spatial data and its distribution were tasks for mapping organisations earning a reputation for producing quality products based on their spatial characteristics, including their visualisation in printed map form to be used for many different types of problems. In contrast, from the second half of the twentieth century(More)
Pyruvate oxidase from Lactobacillus plantarum is a homotetrameric flavoprotein with strong binding sites for FAD, TPP, and a divalent cation. Treatment with acid ammonium sulfate in the presence of 1.5 M KBr leads to the release of the cofactors, yielding the stable apoenzyme. In the present study, the effects of FAD, TPP, and Mn2+ on the structural(More)