Tags

Type your tag names separated by a space and hit enter

Molecular characterization of two galactosemia mutations and one polymorphism: implications for structure-function analysis of human galactose-1-phosphate uridyltransferase.
Biochemistry. 1992 Jun 23; 31(24):5430-3.B

Abstract

We report here the molecular characterization of two galactosemia mutations, L74P and F171S, and one polymorphism, S135L, in human galactose-1-phosphate uridyltransferase (GALT). Both galactosemia mutations result in reduced enzymatic activity when reconstructed in the cDNA and overexpressed. The polymorphism, in contrast, has near normal activity. Both mutations affect evolutionarily conserved residues, suggesting that they are functionally important, while the polymorphism occurs in a nonconserved domain which is presumably not critical for enzymatic function. The F171S mutation is close to the putative active-site nucleophile. Our data further support the notion of molecular heterogeneity of galactosemia and suggest that galactosemia mutations and GALT polymorphisms may be useful tools in highlighting different functional domains in human GALT.

Authors+Show Affiliations

Howard Hughes Medical Institute, Baylor College of Medicine, Houston, Texas 77030-3498.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

1610789

Citation

Reichardt, J K., et al. "Molecular Characterization of Two Galactosemia Mutations and One Polymorphism: Implications for Structure-function Analysis of Human Galactose-1-phosphate Uridyltransferase." Biochemistry, vol. 31, no. 24, 1992, pp. 5430-3.
Reichardt JK, Levy HL, Woo SL. Molecular characterization of two galactosemia mutations and one polymorphism: implications for structure-function analysis of human galactose-1-phosphate uridyltransferase. Biochemistry. 1992;31(24):5430-3.
Reichardt, J. K., Levy, H. L., & Woo, S. L. (1992). Molecular characterization of two galactosemia mutations and one polymorphism: implications for structure-function analysis of human galactose-1-phosphate uridyltransferase. Biochemistry, 31(24), 5430-3.
Reichardt JK, Levy HL, Woo SL. Molecular Characterization of Two Galactosemia Mutations and One Polymorphism: Implications for Structure-function Analysis of Human Galactose-1-phosphate Uridyltransferase. Biochemistry. 1992 Jun 23;31(24):5430-3. PubMed PMID: 1610789.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular characterization of two galactosemia mutations and one polymorphism: implications for structure-function analysis of human galactose-1-phosphate uridyltransferase. AU - Reichardt,J K, AU - Levy,H L, AU - Woo,S L, PY - 1992/6/23/pubmed PY - 1992/6/23/medline PY - 1992/6/23/entrez SP - 5430 EP - 3 JF - Biochemistry JO - Biochemistry VL - 31 IS - 24 N2 - We report here the molecular characterization of two galactosemia mutations, L74P and F171S, and one polymorphism, S135L, in human galactose-1-phosphate uridyltransferase (GALT). Both galactosemia mutations result in reduced enzymatic activity when reconstructed in the cDNA and overexpressed. The polymorphism, in contrast, has near normal activity. Both mutations affect evolutionarily conserved residues, suggesting that they are functionally important, while the polymorphism occurs in a nonconserved domain which is presumably not critical for enzymatic function. The F171S mutation is close to the putative active-site nucleophile. Our data further support the notion of molecular heterogeneity of galactosemia and suggest that galactosemia mutations and GALT polymorphisms may be useful tools in highlighting different functional domains in human GALT. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/1610789/Molecular_characterization_of_two_galactosemia_mutations_and_one_polymorphism:_implications_for_structure_function_analysis_of_human_galactose_1_phosphate_uridyltransferase_ DB - PRIME DP - Unbound Medicine ER -