scholarly journals Substrate recognition by a bifunctional GH30‐7 xylanase B from Talaromyces cellulolyticus

FEBS Open Bio ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 1180-1189 ◽  
Author(s):  
Yusuke Nakamichi ◽  
Masahiro Watanabe ◽  
Akinori Matsushika ◽  
Hiroyuki Inoue
1987 ◽  
Vol 57 (01) ◽  
pp. 017-019 ◽  
Author(s):  
Magda M W Ulrich ◽  
Berry A M Soute ◽  
L Johan M van Haarlem ◽  
Cees Vermeer

SummaryDecarboxylated osteocalcins were prepared and purified from bovine, chicken, human and monkey bones and assayed for their ability to serve as a substrate for vitamin K-dependent carboxylase from bovine liver. Substantial differences were observed, especially between bovine and monkey d-osteocalcin. Since these substrates differ only in their amino acid residues 3 and 4, it seems that these residues play a role in the recognition of a substrate by hepatic carboxylase.


1986 ◽  
Vol 261 (26) ◽  
pp. 11986-11991
Author(s):  
W D Hitz ◽  
P J Card ◽  
K G Ripp

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