Partial primary structure and substrate specificity of proteinase A from Saccharomyces cerevisiae

1985 ◽  
Vol 13 (6) ◽  
pp. 1142-1143 ◽  
Author(s):  
THOMAS DREYER ◽  
IB SVENDSEN ◽  
MARTIN OTTESEN
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Substrate Specificity ◽  
Primary Structure ◽  
Proteinase A

scholarly journals Primary structure of the aspartic proteinase A from Saccharomyces cerevisiae

1986 ◽  
Vol 51 (1) ◽  
pp. 27-41 ◽  
Author(s):  
Thomas Dreyer ◽  
Barbara Halkier ◽  
Ib Svendsen ◽  
Martin Ottesen
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Primary Structure ◽  
Aspartic Proteinase ◽  
Proteinase A

scholarly journals The primary structure of Aspergillus niger acid proteinase A.

1991 ◽  
Vol 266 (29) ◽  
pp. 19480-19483 ◽  
Author(s):  
K. Takahashi ◽  
H. Inoue ◽  
K. Sakai ◽  
T. Kohama ◽  
S. Kitahara ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Primary Structure ◽  
Acid Proteinase ◽  
Proteinase A

PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors

1986 ◽  
Vol 6 (7) ◽  
pp. 2490-2499
Author(s):  
G Ammerer ◽  
C P Hunter ◽  
J H Rothman ◽  
G C Saari ◽  
L A Valls ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Structural Gene ◽  
Yeast Cells ◽  
Linkage Data ◽  
Predicted Amino Acid Sequence ◽  
Multicopy Plasmid ◽  
Proteinase A ◽  
Pep4 Gene ◽  
Cloned Gene

The proteinase A structural gene of Saccharomyces cerevisiae was cloned by using an immunological screening procedure that allows detection of yeast cells which are aberrantly secreting vacuolar proteins (J. H. Rothman, C. P. Hunter, L. A. Valls, and T. H. Stevens, Proc. Natl. Acad. Sci. USA, 83:3248-3252, 1986). A second cloned gene was obtained on a multicopy plasmid by complementation of a pep4-3 mutation. The nucleotide sequences of these two genes were determined independently and were found to be identical. The predicted amino acid sequence of the cloned gene suggests that proteinase A is synthesized as a 405-amino-acid precursor which is proteolytically converted to the 329-amino-acid mature enzyme. Proteinase A shows substantial homology to mammalian aspartyl proteases, such as pepsin, renin, and cathepsin D. The similarities may reflect not only analogous functions but also similar processing and intracellular targeting mechanisms for the two proteins. The cloned proteinase A structural gene, even when it is carried on a single-copy plasmid, complements the deficiency in several vacuolar hydrolase activities that is observed in a pep4 mutant. A strain carrying a deletion in the genomic copy of the gene fails to complement a pep4 mutant of the opposite mating type. Genetic linkage data demonstrate that integrated copies of the cloned proteinase A structural gene map to the PEP4 locus. Thus, the PEP4 gene encodes a vacuolar aspartyl protease, proteinase A, that is required for the in vivo processing of a number of vacuolar zymogens.

scholarly journals Comparative studies on O-acetylhomoserine sulfhydrylase: physiological role and characterization of the Aspergillus nidulans enzyme.

1993 ◽  
Vol 40 (3) ◽  
pp. 421-428 ◽  
Author(s):  
J Brzywczy ◽  
S Yamagata ◽  
A Paszewski
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Substrate Specificity ◽  
Aspergillus Nidulans ◽  
Comparative Studies ◽  
Alternative Pathway ◽  
Physiological Role ◽  
Oligomeric Protein ◽  
Cysteine Synthesis ◽  
Sulfhydryl Compounds

O-acetylhomoserine sulfhydrylase (OAH SHLase) from Aspergillus nidulans is an oligomeric protein with a broad substrate specificity with regard to sulfhydryl compounds. As its Saccharomyces cerevisiae counterpart the enzyme also reacts with O-acetylserine and is inhibited by carbonyl reagents but not by antiserum raised against the yeast enzyme. In contrast to Saccharomyces cerevisiae the enzyme is not essential for Aspergillus nidulans as indicated by the completely prototrophic phenotype of OAH SHLase-negative mutants. Its major physiological role in Aspergillus nidulans seems to be recycling of the thiomethyl group of methylthio-adenosine but it is also a constituent of the alternative pathway of cysteine synthesis.

Substrate Specificity of Non-Pepsin-Type Acid Proteinase, Aspergillus niger Proteinase A

1998 ◽  
pp. 345-348 ◽  
Author(s):  
Shinji Komatsu ◽  
Wataru Nishii ◽  
Hiroshi Sasaki ◽  
Tomonari Muramatsu ◽  
Masaru Tanokura
Keyword(s):  
Aspergillus Niger ◽  
Substrate Specificity ◽  
Acid Proteinase ◽  
Proteinase A
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