Linked Life Data

12783870

Source:http://linkedlifedata.com/resource/pubmed/id/12783870

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
2003-8-25
pubmed:abstractText
The critical step for sorting of lysosomal enzymes is the recognition by a Golgi-located phosphotransferase. The topogenic structure common to all lysosomal enzymes essential for this recognition is still not well defined, except that lysine residues seem to play a critical role. Here we have substituted surface-located lysine residues of lysosomal arylsulfatases A and B. In lysosomal arylsulfatase A only substitution of lysine residue 457 caused a reduction of phosphorylation to 33% and increased secretion of the mutant enzyme. In contrast to critical lysines in various other lysosomal enzymes, lysine 457 is not located in an unstructured loop region but in a helix. It is not strictly conserved among six homologous lysosomal sulfatases. Based on three-dimensional structure comparison, lysines 497 and 507 in arylsulfatase B are in a similar position as lysine 457 of arylsulfatase A. Also, the position of oligosaccharide side chains phosphorylated in arylsulfatase A is similar in arylsulfatase B. Despite the high degree of structural homology between these two sulfatases substitution of lysines 497 and 507 in arylsulfatase B has no effect on the sorting and phosphorylation of this sulfatase. Thus, highly homologous lysosomal arylsulfatases A and B did not develop a single conserved phosphotransferase recognition signal, demonstrating the high variability of this signal even in evolutionary closely related enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32653-61
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12783870-Animals, pubmed-meshheading:12783870-Cell Line, pubmed-meshheading:12783870-Cerebroside-Sulfatase, pubmed-meshheading:12783870-Cricetinae, pubmed-meshheading:12783870-DNA, Complementary, pubmed-meshheading:12783870-Glycosylation, pubmed-meshheading:12783870-Lysine, pubmed-meshheading:12783870-Lysosomes, pubmed-meshheading:12783870-Models, Molecular, pubmed-meshheading:12783870-Mutagenesis, Site-Directed, pubmed-meshheading:12783870-Mutation, pubmed-meshheading:12783870-N-Acetylgalactosamine-4-Sulfatase, pubmed-meshheading:12783870-Oligosaccharides, pubmed-meshheading:12783870-Phosphorylation, pubmed-meshheading:12783870-Precipitin Tests, pubmed-meshheading:12783870-Protein Conformation, pubmed-meshheading:12783870-Protein Structure, Tertiary, pubmed-meshheading:12783870-Transfection, pubmed-meshheading:12783870-Transferases (Other Substituted Phosphate Groups), pubmed-meshheading:12783870-Uridine Diphosphate N-Acetylglucosamine
pubmed:year
2003
pubmed:articleTitle
Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-phosphotransferase.
pubmed:affiliation
Institute of Physiological Chemistry, Rheinische-Friedrich-Wilhelms Universität, Nussallee 11, 53115 Bonn, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't