Linked Life Data

1720313

Source:http://linkedlifedata.com/resource/pubmed/id/1720313

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-1-2
pubmed:databankReference
pubmed:abstractText
We have identified cDNA clones encoding branching enzyme-I (BE-I) from a maize kernel cDNA library. The combined nucleotide sequence of the cDNAs indicates that maize BE-I is initially synthesized as a precursor protein with a putative 64-residue transit peptide at the amino terminus, and that the mature enzyme contains 759 amino acid residues with a calculated molecular mass of 86,236 Da. The four regions, which constitute the catalytic site of amylolytic enzymes, are conserved in the sequences of BE-I and bacterial branching enzymes. This result demonstrates that branching enzyme belongs to a family of the amylolytic enzymes. The BE-I gene is highly expressed in the early stages of kernel development, and the level of the message concentration decreases slowly as kernel maturation proceeds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
181
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
87-94
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Sequence conservation of the catalytic regions of amylolytic enzymes in maize branching enzyme-I.
pubmed:affiliation
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
pubmed:publicationType
Journal Article, Comparative Study