Linked Life Data

10229946

Source:http://linkedlifedata.com/resource/pubmed/id/10229946

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-7-16
pubmed:abstractText
Recently, we identified the maltose inducible alpha-glucosidase MalL of Bacillus subtilis. The malL gene encodes a 561-residue protein with amino acid identities to several alpha-glucosidases and is located in a nine-gene spanning gene cluster, which is presumably organized in an operon. MalL was overproduced, purified, and its enzymatic characteristics were described in more detail. This characterization of the enzyme showed a protein stable up to 37 degrees C after temperature treatment for 15 min and exhibiting an optimal reaction temperature of 42 degrees C. Various disaccharides such as sucrose, maltose, and isomaltose were hydrolyzed with different efficiencies. MalL also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose. MalL expression is subject to both maltose induction and carbon catabolite repression. In this article, we present data demonstrating that induction of MalL expression also occurs when starch, amylose, or glycogen are present in the growth medium. The hydrolysis of these substrates by alpha-amylase presumably leads to products which, when taken up into the cytoplasm, trigger the initiation of maltose operon transcription. Furthermore, MalL expression varies temporally, showing a second induction in the stationary growth phase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amylose, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, http://linkedlifedata.com/resource/pubmed/chemical/Disaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Glycogen, http://linkedlifedata.com/resource/pubmed/chemical/Maltose, http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Starch, http://linkedlifedata.com/resource/pubmed/chemical/Sucrase-Isomaltase Complex, http://linkedlifedata.com/resource/pubmed/chemical/alpha-Glucosidases, http://linkedlifedata.com/resource/pubmed/chemical/maltodextrin, http://linkedlifedata.com/resource/pubmed/chemical/sucrase-isomaltase-maltase
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0923-2508
pubmed:author
pubmed:issnType
Print
pubmed:volume
150
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
167-77
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Properties of maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) in Bacillus subtilis: evidence for its contribution to maltodextrin utilization.
pubmed:affiliation
Lehrstuhl für Mikrobiologie, Universität Erlangen-Nürnberg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't