scholarly journals Substrate Specificity and Subsite Affinities of Crystalline .ALPHA.-Glucosidase from Aspergillus niger.

1991 ◽  
Vol 55 (9) ◽  
pp. 2327-2335 ◽  
Author(s):  
Akihiko KITA ◽  
Hirokazu MATSUI ◽  
Akishige SOMOTO ◽  
Atsuo KIMURA ◽  
Masuhiro TAKATA ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Substrate Specificity ◽  
Alpha Glucosidase

Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger

FEBS Journal ◽  
2005 ◽  
Vol 272 (17) ◽  
pp. 4362-4371 ◽  
Author(s):  
Craig B. Faulds ◽  
Rafael Molina ◽  
Ramon Gonzalez ◽  
Fiona Husband ◽  
Nathalie Juge ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Substrate Specificity ◽  
Feruloyl Esterase

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

scholarly journals Overproduction of .ALPHA.-glucosidase in Aspergillus niger transformed with the cloned gene aglA.

1998 ◽  
Vol 44 (3) ◽  
pp. 177-181 ◽  
Author(s):  
Dong Gun Lee ◽  
Ikuko Nishimura-Masuda ◽  
Akira Nakamura ◽  
Makoto Hidaka ◽  
Haruhiko Masaki ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Cloned Gene ◽  
Alpha Glucosidase

Substrate specificity and subsite affinities of buckwheat .ALPHA.-glucosidase.

1979 ◽  
Vol 43 (2) ◽  
pp. 237-242 ◽  
Author(s):  
Seiya CHIBA ◽  
Ken-ichi KANAYA ◽  
Keitaro HIROMI ◽  
Tokuji SHIMOMURA
Keyword(s):  
Substrate Specificity ◽  
Alpha Glucosidase

Functional analysis of tunicamycin-inducible gene A polypeptide from Aspergillus niger

2005 ◽  
Vol 83 (5) ◽  
pp. 654-658 ◽  
Author(s):  
Yurong Liang ◽  
Wei Li ◽  
Qing Ma ◽  
Yuying Zhang
Keyword(s):  
Functional Analysis ◽  
Aspergillus Niger ◽  
Substrate Specificity ◽  
Protein Disulfide Isomerase ◽  
Ribonuclease A ◽  
Chaperone Activity ◽  
Disulfide Isomerase ◽  
Chaperone Protein ◽  
Protein Disulfide ◽  
Inducible Gene

Tunicamycin-inducible gene A polypeptide (TIGA) is a member of the protein disulfide isomerase (PDI) family and is suggested to facilitate the folding of nascent polypeptides. The functional properties of TIGA were investigated here. TIGA acted as an isomerase, catalyzing the refolding of denatured and reduced ribonuclease A. TIGA also exhibited chaperone activity in the refolding of denatured prochymosin but not in the refolding of glyceraldehyde 3-phosphate dehydrogenase (GAPDH), indicating that it had substrate specificity with respect to chaperone activity. Detailed study with a series of thioredoxin-motif (trx-motif) mutants revealed that the 2 trx-motifs of TIGA were not equal in activity. The N-terminal trx-motif was more active than the C-terminal trx-motif, and the first cysteine in each trx-motif was necessary for isomerase activity.Key words: tunicamycin-inducible gene A polypeptide (TIGA), protein disulfide isomerase, chaperone, protein refolding.

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