Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1989-10-24
pubmed:abstractText
A Ca2+ binding site like an EF-hand motif was designed and created in human lysozyme by replacing both Gln-86 and Ala-92 with aspartic acids by site-directed mutagenesis. The mutant human lysozyme (D86/92-lysozyme) was expressed and secreted by yeast. One Ca2+ was found to bind one molecule of the purified protein with the binding constant 5.0 x 10(6) M-1. The enzymatic activity of holo-D86/92-lysozyme against glycol chitin at 40 degrees C was 2-fold higher than that of the native lysozyme. Maximal activity of the holo-D86/92-lysozyme was observed at 80 degrees C, where its relative activity normalized to the value at 40 degrees C was 6-fold and 17-fold higher than those of the native and apoenzymes, respectively. The activities of the native lysozyme and apo-D86/92-lysozyme were maximum at 65 degrees C-70 degrees C. Moreover, D86/92-lysozyme was more stable against protease digestion than the native lysozyme. These results indicate that the creation of the calcium binding site like an EF-hand motif in the human lysozyme enhances its structural stability.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-1142432, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-13650640, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3059346, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3072018, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3109419, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3118211, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3200317, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3214551, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3288200, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3299367, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3666156, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3783715, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3785375, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-3974698, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-4382800, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-4530293, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-4570606, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-4700463, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-5229853, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-5532231, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-5532232, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-6225933, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-6387910, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-6709045, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-6774718, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-6866082, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-7207627, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-7260958, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-7277500, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-7334520, http://linkedlifedata.com/resource/pubmed/commentcorrection/2674939-7378374
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6903-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Design and creation of a Ca2+ binding site in human lysozyme to enhance structural stability.
pubmed:affiliation
Protein Engineering Research Institute, Osaka, Japan.
pubmed:publicationType
Journal Article, Comparative Study