Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family. 2004

Jonna Lehtonen, and Bairong Shen, and Mauno Vihinen, and Angela Casini, and Andrea Scozzafava, and Claudiu T Supuran, and Anna-Kaisa Parkkila, and Juha Saarnio, and Antti J Kivelä, and Abdul Waheed, and William S Sly, and Seppo Parkkila
Institute of Medical Technology, University of Tampere, Tampere, Finland.

The carbonic anhydrase (CA) gene family has been reported to consist of at least 11 enzymatically active members and a few inactive homologous proteins. Recent analyses of human and mouse databases provided evidence that human and mouse genomes contain genes for still another novel CA isozyme hereby named CA XIII. In the present study, we modeled the structure of human CA XIII. This model revealed a globular molecule with high structural similarity to cytosolic isozymes, CA I, II, and III. Recombinant mouse CA XIII showed catalytic activity similar to those of mitochondrial CA V and cytosolic CA I, with k(cat)/K(m) of 4.3 x 10(7) m(-1) s(-1), and k(cat) of 8.3 x 10(4) s(-1). It is very susceptible to inhibition by sulfonamide and anionic inhibitors, with inhibition constants of 17 nm for acetazolamide, a clinically used sulfonamide, and of 0.25 microm, for cyanate, respectively. Using panels of cDNAs we evaluated human and mouse CA13 gene expression in a number of different tissues. In human tissues, positive signals were identified in the thymus, small intestine, spleen, prostate, ovary, colon, and testis. In mouse, positive tissues included the spleen, lung, kidney, heart, brain, skeletal muscle, and testis. We also investigated the cellular and subcellular localization of CA XIII in human and mouse tissues using an antibody raised against a polypeptide of 14 amino acids common for both human and mouse orthologues. Immunohistochemical staining showed a unique and widespread distribution pattern for CA XIII compared with the other cytosolic CA isozymes. In conclusion, the predicted amino acid sequence, structural model, distribution, and activity data suggest that CA XIII represents a novel enzyme, which may play important physiological roles in several organs.

UI MeSH Term Description Entries
D007527 Isoenzymes Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009928 Organ Specificity Characteristic restricted to a particular organ of the body, such as a cell type, metabolic response or expression of a particular protein or antigen. Tissue Specificity,Organ Specificities,Specificities, Organ,Specificities, Tissue,Specificity, Organ,Specificity, Tissue,Tissue Specificities
D002256 Carbonic Anhydrases A family of zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide. They play an important role in the transport of CARBON DIOXIDE from the tissues to the LUNG. EC 4.2.1.1. Carbonate Dehydratase,Carbonic Anhydrase,Anhydrases, Carbonic,Dehydratase, Carbonate
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

Jonna Lehtonen, and Bairong Shen, and Mauno Vihinen, and Angela Casini, and Andrea Scozzafava, and Claudiu T Supuran, and Anna-Kaisa Parkkila, and Juha Saarnio, and Antti J Kivelä, and Abdul Waheed, and William S Sly, and Seppo Parkkila
April 2005, BMC cancer,
Jonna Lehtonen, and Bairong Shen, and Mauno Vihinen, and Angela Casini, and Andrea Scozzafava, and Claudiu T Supuran, and Anna-Kaisa Parkkila, and Juha Saarnio, and Antti J Kivelä, and Abdul Waheed, and William S Sly, and Seppo Parkkila
August 2006, Bioorganic & medicinal chemistry letters,
Jonna Lehtonen, and Bairong Shen, and Mauno Vihinen, and Angela Casini, and Andrea Scozzafava, and Claudiu T Supuran, and Anna-Kaisa Parkkila, and Juha Saarnio, and Antti J Kivelä, and Abdul Waheed, and William S Sly, and Seppo Parkkila
November 2004, Bioorganic & medicinal chemistry letters,
Jonna Lehtonen, and Bairong Shen, and Mauno Vihinen, and Angela Casini, and Andrea Scozzafava, and Claudiu T Supuran, and Anna-Kaisa Parkkila, and Juha Saarnio, and Antti J Kivelä, and Abdul Waheed, and William S Sly, and Seppo Parkkila
January 2007, Current topics in medicinal chemistry,
Jonna Lehtonen, and Bairong Shen, and Mauno Vihinen, and Angela Casini, and Andrea Scozzafava, and Claudiu T Supuran, and Anna-Kaisa Parkkila, and Juha Saarnio, and Antti J Kivelä, and Abdul Waheed, and William S Sly, and Seppo Parkkila
October 2001, The Journal of veterinary medical science,
Jonna Lehtonen, and Bairong Shen, and Mauno Vihinen, and Angela Casini, and Andrea Scozzafava, and Claudiu T Supuran, and Anna-Kaisa Parkkila, and Juha Saarnio, and Antti J Kivelä, and Abdul Waheed, and William S Sly, and Seppo Parkkila
November 2003, The Journal of veterinary medical science,
Jonna Lehtonen, and Bairong Shen, and Mauno Vihinen, and Angela Casini, and Andrea Scozzafava, and Claudiu T Supuran, and Anna-Kaisa Parkkila, and Juha Saarnio, and Antti J Kivelä, and Abdul Waheed, and William S Sly, and Seppo Parkkila
January 2010, Current pharmaceutical design,
Jonna Lehtonen, and Bairong Shen, and Mauno Vihinen, and Angela Casini, and Andrea Scozzafava, and Claudiu T Supuran, and Anna-Kaisa Parkkila, and Juha Saarnio, and Antti J Kivelä, and Abdul Waheed, and William S Sly, and Seppo Parkkila
July 2004, Bioorganic & medicinal chemistry letters,
Jonna Lehtonen, and Bairong Shen, and Mauno Vihinen, and Angela Casini, and Andrea Scozzafava, and Claudiu T Supuran, and Anna-Kaisa Parkkila, and Juha Saarnio, and Antti J Kivelä, and Abdul Waheed, and William S Sly, and Seppo Parkkila
May 1999, The Journal of biological chemistry,
Jonna Lehtonen, and Bairong Shen, and Mauno Vihinen, and Angela Casini, and Andrea Scozzafava, and Claudiu T Supuran, and Anna-Kaisa Parkkila, and Juha Saarnio, and Antti J Kivelä, and Abdul Waheed, and William S Sly, and Seppo Parkkila
August 2016, Gene,
Copied contents to your clipboard!