Studies on the regulation of the human E1 subunit of the 2-oxoglutarate dehydrogenase complex, including the identification of a novel calcium-binding site

2014 ◽  
Vol 459 (2) ◽  
pp. 369-381 ◽  
Author(s):  
Craig T. Armstrong ◽  
J. L. Ross Anderson ◽  
Richard M. Denton
Keyword(s):  
Energy Metabolism ◽  
Binding Site ◽  
Calcium Binding ◽  
Adenine Nucleotides ◽  
Calcium Binding Site ◽  
Site Of Action ◽  
Oxoglutarate Dehydrogenase ◽  
Dehydrogenase Complex

The oxoglutarate dehydrogenase complex regulates energy metabolism through its sensitivity to adenine nucleotides, NADH and Ca2+. In the present study, we show definitively that the E1 subunit is the site of action for these regulators, and identify the Ca2+-binding site.

scholarly journals A disulfide bridge in the calcium binding site of a polyester hydrolase increases its thermal stability and activity against polyethylene terephthalate

FEBS Open Bio ◽  
2016 ◽  
Vol 6 (5) ◽  
pp. 425-432 ◽  
Author(s):  
Johannes Then ◽  
Ren Wei ◽  
Thorsten Oeser ◽  
André Gerdts ◽  
Juliane Schmidt ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Binding Site ◽  
Polyethylene Terephthalate ◽  
Calcium Binding ◽  
Disulfide Bridge ◽  
Calcium Binding Site

Calcium-Binding Site β2, Adjacent to the “b” Polymerization Site, Modulates Lateral Aggregation of Protofibrils during Fibrin Polymerization†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (9) ◽  
pp. 2475-2483 ◽  
Author(s):  
Michael S. Kostelansky ◽  
Karim C. Lounes ◽  
Li Fang Ping ◽  
Sarah K. Dickerson ◽  
Oleg V. Gorkun ◽  
...  
Keyword(s):  
Binding Site ◽  
Calcium Binding ◽  
Calcium Binding Site ◽  
Fibrin Polymerization

scholarly journals The calcium-binding site of human glutamate carboxypeptidase II is critical for dimerization, thermal stability, and enzymatic activity

2018 ◽  
Vol 27 (9) ◽  
pp. 1575-1584 ◽  
Author(s):  
Jakub Ptacek ◽  
Jana Nedvedova ◽  
Michal Navratil ◽  
Barbora Havlinova ◽  
Jan Konvalinka ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Enzymatic Activity ◽  
Binding Site ◽  
Calcium Binding ◽  
Calcium Binding Site ◽  
Glutamate Carboxypeptidase Ii ◽  
Glutamate Carboxypeptidase

scholarly journals Structural and Functional Characterization of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance

2019 ◽  
Vol 20 (19) ◽  
pp. 4902 ◽  
Author(s):  
Christian Roth ◽  
Olga V. Moroz ◽  
Johan P. Turkenburg ◽  
Elena Blagova ◽  
Jitka Waterman ◽  
...  
Keyword(s):  
Binding Site ◽  
Calcium Binding ◽  
Functional Characterization ◽  
Industrial Applications ◽  
Glycoside Hydrolases ◽  
Industrial Processes ◽  
Calcium Binding Site ◽  
Ph Tolerance ◽  
Speed Up ◽  
Binding Cleft

Amylases are probably the best studied glycoside hydrolases and have a huge biotechnological value for industrial processes on starch. Multiple amylases from fungi and microbes are currently in use. Whereas bacterial amylases are well suited for many industrial processes due to their high stability, fungal amylases are recognized as safe and are preferred in the food industry, although they lack the pH tolerance and stability of their bacterial counterparts. Here, we describe three amylases, two of which have a broad pH spectrum extending to pH 8 and higher stability well suited for a broad set of industrial applications. These enzymes have the characteristic GH13 α-amylase fold with a central (β/α)8-domain, an insertion domain with the canonical calcium binding site and a C-terminal β-sandwich domain. The active site was identified based on the binding of the inhibitor acarbose in form of a transglycosylation product, in the amylases from Thamnidium elegans and Cordyceps farinosa. The three amylases have shortened loops flanking the nonreducing end of the substrate binding cleft, creating a more open crevice. Moreover, a potential novel binding site in the C-terminal domain of the Cordyceps enzyme was identified, which might be part of a starch interaction site. In addition, Cordyceps farinosa amylase presented a successful example of using the microseed matrix screening technique to significantly speed-up crystallization.

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