The Relationship of Discrete Amino Acid Regions to the Biochemical Properties of Human Phenol Sulfotransferases (SULTs)
type: CreativeWork
description: Sulfation is important in the metabolism of many different compounds including phenols, monoamine neurotransmitters, steroid and thyroid hormones, and numerous xenobiotics. The addition of the sulfuryl moiety to substrates produces effects such as increased water solubility and renal excretion, decreased activity, activation of certain agents, and formation of unstable esters that react with DNA to form adducts. The most studied form of the sulfotransferase (STILT) enzymes in humans is SULT1 Al. Allozymes (expressed allelic variants) of SULT1A1 have been detected in human blood platelets at different proportions in separate ethnic populations. The SULT1A1 level of activity and thermal stability measured in the human population are variable. Allozymes are associated with the variability measured in human SULT1 Al activities and thermal stability. The reason for the catalytic differences is not completely understood, but low STJLT1 Al activity may increase susceptability to toxins due to an individual’s inability to metabolize specific reagents. The super-family of human SULT enzymes is classified according to amino acid sequence differences. SULT1 Al and STJLT1 A3 are 93% similar in their amino acid sequences, but they differ in biochemical properties including substrate specificity and thermal stability. To gain knowledge of amino acids that affect the different biochemical properties we produced chimeric and mutant SULT1A1 and SULT1A3 enzymes. Specific amino acid residues over the length of the protein affect the biochemical properties of the SULTl A1 and SULT1 A3 enzymes. The N-terrninal portion of the SULT1A1 enzyme is important for measurable activity of the enzyme because when mutated to the residues present in the N-terminus of SULTl A3, no activity is detectable. The presence of the N-terminal of SULTl A1 with the center region of SUI,T1 A3 creates a more hydrophilic protein with greater thermal stability and resistance to NaCl inhibition for these chimeric p…
abstract: Sulfation is important in the metabolism of many different compounds including phenols, monoamine neurotransmitters, steroid and thyroid hormones, and numerous xenobiotics. The addition of the sulfuryl moiety to substrates produces effects such as increased water solubility and renal excretion, decreased activity, activation of certain agents, and formation of unstable esters that react with DNA to form adducts. The most studied form of the sulfotransferase (STILT) enzymes in humans is SULT1 Al. Allozymes (expressed allelic variants) of SULT1A1 have been detected in human blood platelets at different proportions in separate ethnic populations. The SULT1A1 level of activity and thermal stability measured in the human population are variable. Allozymes are associated with the variability measured in human SULT1 Al activities and thermal stability. The reason for the catalytic differences is not completely understood, but low STJLT1 Al activity may increase susceptability to toxins due to an individual’s inability to metabolize specific reagents. The super-family of human SULT enzymes is classified according to amino acid sequence differences. SULT1 Al and STJLT1 A3 are 93% similar in their amino acid sequences, but they differ in biochemical properties including substrate specificity and thermal stability. To gain knowledge of amino acids that affect the different biochemical properties we produced chimeric and mutant SULT1A1 and SULT1A3 enzymes. Specific amino acid residues over the length of the protein affect the biochemical properties of the SULTl A1 and SULT1 A3 enzymes. The N-terrninal portion of the SULT1A1 enzyme is important for measurable activity of the enzyme because when mutated to the residues present in the N-terminus of SULTl A3, no activity is detectable. The presence of the N-terminal of SULTl A1 with the center region of SUI,T1 A3 creates a more hydrophilic protein with greater thermal stability and resistance to NaCl inhibition for these chimeric p…
author: Kudeacek, Patrick Eugene
language: en_US
date published: 2001
date modified: 2026-07-24T01:50:02Z
provider: Creighton University
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: Creighton University

PropertyValue
property ID: Handle
value: http://hdl.handle.net/10504/65479