Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-3-2
pubmed:databankReference
pubmed:abstractText
The alpha-amylase gene (amy) of Streptomyces lividans TK24 was cloned in an amylase deficient mutant strain S. lividans M2. The cloned gene contained an open reading frame (ORF) of 2757 nucleotides (919 amino acids) coding for a protein of 100 kDa. Sequencing of the amino terminus of the extracellular alpha-amylase protein revealed the presence of a signal peptide of 33 amino acid residues. The transcriptional initiation site was mapped by the primer extension method with T4 DNA polymerase and was found to be transcribed from an unique promoter. The alpha-amylase protein produced by S. lividans was larger than those derived from other origins. It also contained the four common conserved regions characteristic of other alpha-amylase proteins.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
1171
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
255-62
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Cloning and characterization of an alpha-amylase gene from Streptomyces lividans.
pubmed:affiliation
Culture Collection and Research Center, Food Industry Research and Development Institute, Hsinchu, Taiwan, R.O.C.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't