Linked Life Data

8024558

Source:http://linkedlifedata.com/resource/pubmed/id/8024558

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-8-1
pubmed:abstractText
Twelve tyrosines, ten glutamates, and five histidines were individually substituted for phenylalanine, glutamine, and asparagine, respectively, in the beta-galactosidase from Lactobacillus delbrückii subsp. bulgaricus. Only Y509, E464, H351, and H534 appear to be essential for the activity of the enzyme. The residues Y509 and E464 are homologous to Y503 and E461, respectively, of the Escherichia coli lacZ beta-galactosidase which have been shown to be necessary for its activity. Surprisingly, a number of amino acids that are highly conserved in the sequence alignments of nine beta-galactosidases and four beta-glucuronidases are not essential for enzyme activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
201
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1167-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Two histidines are essential for the activity of the beta-galactosidase from Lactobacillus delbrückii subsp. bulgaricus.
pubmed:affiliation
Genencor International, Inc., South San Francisco, California 94080.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't