|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5
|
|
pubmed:dateCreated |
1995-7-27
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
A cDNA for proctase B from Aspergillus niger var. macrosporus was isolated and sequenced. The deduced amino acid sequence (394 residues) of the preproform of the enzyme was highly homologous (98% identify) with those of aspergillopepsins I from A. awamori and A. saitoi, and moderately homologous (68% identity) with that of A. oryzae. Most of the sequence differences were found in the carboxyl-terminal domain.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
B
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0916-8451
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
59
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
954-5
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:7787314-Amino Acid Sequence,
pubmed-meshheading:7787314-Aspartic Acid Endopeptidases,
pubmed-meshheading:7787314-Aspergillus niger,
pubmed-meshheading:7787314-Base Sequence,
pubmed-meshheading:7787314-Cloning, Molecular,
pubmed-meshheading:7787314-DNA, Complementary,
pubmed-meshheading:7787314-Molecular Sequence Data,
pubmed-meshheading:7787314-Protein Conformation,
pubmed-meshheading:7787314-Sequence Homology, Amino Acid,
pubmed-meshheading:7787314-Sequence Homology, Nucleic Acid,
pubmed-meshheading:7787314-Structure-Activity Relationship
|
|
pubmed:year |
1995
|
|
pubmed:articleTitle |
Molecular cloning of a cDNA for proctase B from Aspergillus niger var. macrosporus and sequence comparison with other aspergillopepsins I.
|
|
pubmed:affiliation |
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study
|
