| Structure and function in galactosyltransferase. Sequence locations of alpha-lactalbumin binding site, thiol groups, and disulfide bond. | |
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MedLine Citation:
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PMID: 1898734 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The region(s) of bovine galactosyltransferase that interacts with the lactose synthase regulatory protein alpha-lactalbumin was investigated using trace 3H acetylation to probe the effects of alpha-lactalbumin on the reactivities of the individual amino groups of galactosyltransferase. In the presence of Mn2+, alpha-lactalbumin was found to reduce the reactivities of lysines 93 and 181 and to increase the reactivities of one or more of lysines 230, 237, and 241. The addition of N-acetylglucosamine (20 mM), which enhances complex formation between the two proteins, did not significantly alter the pattern of perturbation. These results indicate that the NH2-terminal region of the catalytic domain of galactosyltransferase, and possibly part of the proline-rich "stem" region, is affected by the association with alpha-lactalbumin and is therefore implicated in the binding of acceptor substrates. In a separate study only cysteines 176, 266, and 342 of galactosyltransferase were found to react with [3H]iodoacetic acid under denaturing conditions. From their lack of reactivity it is deduced that the remaining two cysteines, residues 134 and 247, are joined in a disulfide linkage. From these results and those of a previous study of UDP-galactose binding (Yadav, S., and Brew, K. (1990) J. Biol. Chem. 265, 14163-14169) it appears that the soluble form of galactosyltransferase is composed of two domains, the NH2-terminal 150 residues containing the Cys134-Cys247 disulfide bond, which functions in alpha-lactalbumin and acceptor binding, and the COOH-terminal region, which is involved in UDP-galactose binding. |
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Authors:
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S P Yadav; K Brew |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 266 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1991 Jan |
Date Detail:
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Created Date: 1991-02-12 Completed Date: 1991-02-12 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 698-703 Citation Subset: IM |
Affiliation:
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Department of Biochemistry and Molecular Biology, University of Miami, Florida 33136. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Amino Acids / chemistry Animals Binding Sites Cattle Chromatography, High Pressure Liquid Cysteine / metabolism Disulfides / metabolism Galactosyltransferases / metabolism* Lactalbumin / metabolism* Molecular Sequence Data Structure-Activity Relationship Sulfhydryl Compounds / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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GM21363/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Disulfides; 0/Sulfhydryl Compounds; 52-90-4/Cysteine; 9013-90-5/Lactalbumin; EC 2.4.1.-/Galactosyltransferases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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