rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2-3
|
pubmed:dateCreated |
2000-3-3
|
pubmed:abstractText |
A cDNA encoding 1,2-alpha-D-mannosidase mds 1 from Trichoderma reesei was cloned. The largest open reading frame occupied 1571 bp. The predicted sequence contains 523 amino acid residues for a calculated molecular mass of 56,266 Da and shows high similarity to the amino acid sequences of 1,2-alpha-D-mannosidases from Aspergillus saitoi and Penicillium citrinum (51.6 and 51.0% identity, respectively). T. reesei mannosidase was produced as a recombinant enzyme in the yeast Pichia pastoris. Replacement of the N-terminal part with the prepro-signal peptide of the Saccharomyces cerevisiae alpha-mating factor resulted in high amounts of secreted enzyme. A three-step purification protocol was designed and the enzymatic properties were analyzed. The enzyme was characterized as a class-I mannosidase.
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0168-1656
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
17
|
pubmed:volume |
77
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
255-63
|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10682284-Amino Acid Sequence,
pubmed-meshheading:10682284-Aspergillus,
pubmed-meshheading:10682284-Cloning, Molecular,
pubmed-meshheading:10682284-DNA, Complementary,
pubmed-meshheading:10682284-Mannosidases,
pubmed-meshheading:10682284-Molecular Sequence Data,
pubmed-meshheading:10682284-Penicillium,
pubmed-meshheading:10682284-Peptides,
pubmed-meshheading:10682284-Pichia,
pubmed-meshheading:10682284-Protein Sorting Signals,
pubmed-meshheading:10682284-Recombinant Fusion Proteins,
pubmed-meshheading:10682284-Recombinant Proteins,
pubmed-meshheading:10682284-Saccharomyces cerevisiae,
pubmed-meshheading:10682284-Sequence Alignment,
pubmed-meshheading:10682284-Trichoderma
|
pubmed:year |
2000
|
pubmed:articleTitle |
Molecular cloning and enzymatic characterization of a Trichoderma reesei 1,2-alpha-D-mannosidase.
|
pubmed:affiliation |
Department of Molecular Biology, Flanders Interuniversity Institute for Biotechnology, Ghent, Belgium.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|