Linked Life Data

10502668

Source:http://linkedlifedata.com/resource/pubmed/id/10502668

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1999-12-30
pubmed:abstractText
Renin binding protein (RnBP) is a proteinous renin inhibitor firstly isolated from porcine kidney. Recently, the protein was identified as the enzyme, N-acetyl-D-glucosamine (GlcNAc) 2-epimerase. The GlcNAc 2-epimerase activity of recombinant human RnBP was specifically inhibited by SH-reagents such as N-ethylmaleimide, 5, 5'-dithiobis-2-nitrobenzoate, and iodoacetic acid, indicating that the most probable reactive site is a cysteine residue. To identify the active site residue(s), we have constructed ten cysteine residue mutants (C41S, C66S, C104S, C125S, C210S, C239S, C302S, C380S, C386S, and C390S) for human GlcNAc 2-epimerase and expressed them in Escherichia coli cells. The relative specific activities of C41S, C66S, C125S, C210S, C239S, C302S, C386S, and C390S are nearly the same to that of the wild-type enzyme. The specific activity of the C104S mutant is 26% of that of the wild-type enzyme. The expression of the C380S mutant in E. coli cells was detected on Western blotting, whereas GlcNAc 2-epimerase activity was not detected in the extract. These results indicate that Cys380 is essential for the enzymatic activity of human GlcNAc 2-epimerase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
126
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
639-42
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein).
pubmed:affiliation
Department of Bioengineering, Akita Research Institute of Food and Brewing (ARIF), Arayamachi, Akita, 010-1623, Japan. saori@arif.pref. akita.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't