Dual substrate recognition of aminotransferases

2005 ◽  
Vol 5 (3) ◽  
pp. 160-172 ◽  
Author(s):  
Ken Hirotsu ◽  
Masaru Goto ◽  
Akihiro Okamoto ◽  
Ikuko Miyahara
Keyword(s):  
Substrate Recognition ◽  
Dual Substrate

scholarly journals Quantum Chemical Study of Dual-Substrate Recognition in ω-Transaminase

ACS Omega ◽  
2017 ◽  
Vol 2 (3) ◽  
pp. 890-898 ◽  
Author(s):  
Bianca Manta ◽  
Karim Engelmark Cassimjee ◽  
Fahmi Himo
Keyword(s):  
Quantum Chemical ◽  
Substrate Recognition ◽  
Quantum Chemical Study ◽  
Chemical Study ◽  
Dual Substrate

Substrate Recognition Mechanism of Thermophilic Dual-Substrate Enzyme

2001 ◽  
Vol 130 (1) ◽  
pp. 89-98 ◽  
Author(s):  
H. Ura ◽  
T. Nakai ◽  
S.-i. Kawaguchi ◽  
I. Miyahara ◽  
K. Hirotsu ◽  
...  
Keyword(s):  
Substrate Recognition ◽  
Recognition Mechanism ◽  
Dual Substrate

scholarly journals Structural and biochemical characterization of the dual substrate recognition of the (R)-selective amine transaminase fromAspergillus fumigatus

FEBS Journal ◽  
2014 ◽  
Vol 282 (2) ◽  
pp. 407-415 ◽  
Author(s):  
Lilly Skalden ◽  
Maren Thomsen ◽  
Matthias Höhne ◽  
Uwe T. Bornscheuer ◽  
Winfried Hinrichs
Keyword(s):  
Biochemical Characterization ◽  
Substrate Recognition ◽  
Dual Substrate

Bacillus anthracis ω-amino acid:pyruvate transaminase employs a different mechanism for dual substrate recognition than other amine transaminases

2016 ◽  
Vol 100 (10) ◽  
pp. 4511-4521 ◽  
Author(s):  
Fabian Steffen-Munsberg ◽  
Philipp Matzel ◽  
Miriam A. Sowa ◽  
Per Berglund ◽  
Uwe T. Bornscheuer ◽  
...  
Keyword(s):  
Bacillus Anthracis ◽  
Substrate Recognition ◽  
Dual Substrate

Substrate Recognition by Vitamin K-Dependent Carboxylase

1987 ◽  
Vol 57 (01) ◽  
pp. 017-019 ◽  
Author(s):  
Magda M W Ulrich ◽  
Berry A M Soute ◽  
L Johan M van Haarlem ◽  
Cees Vermeer
Keyword(s):  
Amino Acid ◽  
Vitamin K ◽  
Substrate Recognition ◽  
Bovine Liver ◽  
Amino Acid Residues

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.

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