Molecular cloning and expression of a guinea pig 3-hydroxysteroid sulfotransferase distinct from chiral-specific 3 alpha-hydroxysteroid sulfotransferase. 1995

N X Luu, and W J Driscoll, and B M Martin, and C A Strott
Section on Steroid Regulation, Endocrinology and Reproduction Research Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-4510, USA.

A guinea pig adrenal hydroxysteroid sulfotransferase (gpHST2) has been cloned that is distinct from guinea pig hydroxysteroid sulfotransferase that stereoselectively acts on 3 alpha-hydroxylated neutral steroids (gp3 alpha HST, redesignated gpHST1). The deduced amino acid sequences for gpHST1 and gpHST2 are 86% identical; however, whereas gpHST1 selectively acts on 3 alpha-hydroxylated steroids, gpHST2 demonstrates a clear preference (but not exclusive specificity) for 3 beta-hydroxylated steroids suggesting that gpHST2 is similar to a previously reported guinea pig hydroxysteroid sulfotransferase that selectively acts on 3 beta-hydroxylated neutral steroids (gp3 beta HST). Additionally, gpHST2 (33K) is the same size as gp3 beta HST and larger than gpHST1 (32K), contains amino acid sequences identical to peptides obtained from gp3 beta HST and cross-reacts with antibodies raised against purified gp3 beta HST. Nonetheless, gpHST2 can sulfonate both 3 alpha- and 3 beta-hydroxylated neutral steroids, suggesting that either gp3 beta HST does not have the exquisite stereoselectivity previously indicated or this subfamily of hydroxysteroid sulfotransferases is larger than originally thought.

UI MeSH Term Description Entries
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
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
D006168 Guinea Pigs A common name used for the genus Cavia. The most common species is Cavia porcellus which is the domesticated guinea pig used for pets and biomedical research. Cavia,Cavia porcellus,Guinea Pig,Pig, Guinea,Pigs, Guinea
D000311 Adrenal Glands A pair of glands located at the cranial pole of each of the two KIDNEYS. Each adrenal gland is composed of two distinct endocrine tissues with separate embryonic origins, the ADRENAL CORTEX producing STEROIDS and the ADRENAL MEDULLA producing NEUROTRANSMITTERS. Adrenal Gland,Gland, Adrenal,Glands, Adrenal
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
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D015238 Sulfotransferases Enzymes which transfer sulfate groups to various acceptor molecules. They are involved in posttranslational sulfation of proteins and sulfate conjugation of exogenous chemicals and bile acids. EC 2.8.2. Sulfotransferase
D016415 Sequence Alignment The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms. Sequence Homology Determination,Determination, Sequence Homology,Alignment, Sequence,Alignments, Sequence,Determinations, Sequence Homology,Sequence Alignments,Sequence Homology Determinations
D017386 Sequence Homology, Amino Acid The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species. Homologous Sequences, Amino Acid,Amino Acid Sequence Homology,Homologs, Amino Acid Sequence,Homologs, Protein Sequence,Homology, Protein Sequence,Protein Sequence Homologs,Protein Sequence Homology,Sequence Homology, Protein,Homolog, Protein Sequence,Homologies, Protein Sequence,Protein Sequence Homolog,Protein Sequence Homologies,Sequence Homolog, Protein,Sequence Homologies, Protein,Sequence Homologs, Protein

Related Publications

N X Luu, and W J Driscoll, and B M Martin, and C A Strott
June 1994, The Journal of biological chemistry,
N X Luu, and W J Driscoll, and B M Martin, and C A Strott
June 1991, Molecular endocrinology (Baltimore, Md.),
N X Luu, and W J Driscoll, and B M Martin, and C A Strott
April 1998, Journal of biochemistry,
N X Luu, and W J Driscoll, and B M Martin, and C A Strott
August 1992, Molecular endocrinology (Baltimore, Md.),
N X Luu, and W J Driscoll, and B M Martin, and C A Strott
December 1995, Brain research. Molecular brain research,
N X Luu, and W J Driscoll, and B M Martin, and C A Strott
August 2001, European journal of pharmacology,
N X Luu, and W J Driscoll, and B M Martin, and C A Strott
November 1993, The Journal of biological chemistry,
N X Luu, and W J Driscoll, and B M Martin, and C A Strott
February 1997, The Journal of biological chemistry,
N X Luu, and W J Driscoll, and B M Martin, and C A Strott
August 1992, Biochemical and biophysical research communications,
Copied contents to your clipboard!